EzCatDB: M00152
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00152
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.10.25.10 : Laminin
Domain 22.40.20.10 : Plasminogen Kringle 4
Domain 32.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 42.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.73

CATH domainRelated DB codes (homologues)
2.10.25.10 : LamininM00139,M00133,M00212,M00155,M00315,M00316
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411
2.40.20.10 : Plasminogen Kringle 4M00155,M00157

Enzyme Name
UniProtKBKEGG

P00749
Protein nameUrokinase-type plasminogen activatoru-plasminogen activator
urokinase
urinary plasminogen activator
cellular plasminogen activator
urokinase-type plasminogen activator
double-chain urokinase-type plasminogen activator
two-chain urokinase-type plasminogen activator
urokinase plasminogen activator
uPA
u-PA
abbokinase
urinary esterase A
SynonymsU-plasminogen activator
uPA
EC 3.4.21.73
ContainsUrokinase-type plasminogen activator long chain A
Urokinase-type plasminogen activator short chain A
Urokinase-type plasminogen activator chain B
RefSeqNP_001138503.1 (Protein)
NM_001145031.1 (DNA/RNA sequence)
NP_002649.1 (Protein)
NM_002658.3 (DNA/RNA sequence)
MEROPSS01.231 (Serine)
PfamPF00051 (Kringle)
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP00749
Entry nameUROK_HUMAN
ActivitySpecific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
SubunitFound in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Binds LRP1B, binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR.
Subcellular locationSecreted.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00520C00001C00471I00087I00085I00086
CompoundPlasminogenH2OPlasminPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
962
22247451




              
1urkA01Unbound UnboundUnboundUnboundUnbound
1urkA02Unbound UnboundUnboundUnboundUnbound
1kduAUnbound UnboundUnboundUnboundUnbound
1c5wB01Unbound Analogue:ESIUnboundUnboundUnbound
1c5xB01Unbound Analogue:ESIUnboundUnboundUnbound
1c5yB01Unbound Analogue:ESPUnboundUnboundUnbound
1c5zB01Unbound Analogue:BAMUnboundUnboundUnbound
1ejnA01Analogue:AGB UnboundUnboundUnboundUnbound
1f5lA01Unbound Analogue:AMRUnboundUnboundUnbound
1f92A01Unbound Analogue:UKPUnboundUnboundUnbound
1fv9A01Unbound Analogue:172UnboundUnboundUnbound
1gi7B01Unbound Analogue:120UnboundUnboundUnbound
1gi8B01Analogue:BMZ UnboundUnboundUnboundUnbound
1gi9B01Analogue:123 UnboundUnboundUnboundUnbound
1gj7B01Analogue:132 UnboundUnboundUnboundUnbound
1gj8B01Analogue:133 UnboundUnboundUnboundUnbound
1gj9B01Analogue:134 UnboundUnboundUnboundUnbound
1gjaB01Analogue:135 UnboundUnboundUnboundUnbound
1gjbB01Analogue:130 UnboundUnboundUnboundUnbound
1gjcB01Analogue:130 UnboundUnboundUnboundUnbound
1gjdB01Analogue:136 UnboundUnboundUnboundUnbound
1lmwB01Unbound UnboundUnboundUnboundTransition-state-analogue:GLU-GLY-MAI(chain I)
1lmwD01Unbound UnboundUnboundUnboundTransition-state-analogue:GLU-GLY-MAI(chain J)
1o3pB01Analogue:655 UnboundUnboundUnboundUnbound
1owdA01Analogue:497 UnboundUnboundUnboundUnbound
1oweA01Analogue:675 UnboundUnboundUnboundUnbound
1owhA01Analogue:239 UnboundUnboundUnboundUnbound
1owiA01Analogue:426 UnboundUnboundUnboundUnbound
1owjA01Analogue:155 UnboundUnboundUnboundUnbound
1owkA01Analogue:303 UnboundUnboundUnboundUnbound
1c5wB02Unbound UnboundUnboundUnboundUnbound
1c5xB02Unbound UnboundUnboundUnboundUnbound
1c5yB02Unbound UnboundUnboundUnboundUnbound
1c5zB02Unbound UnboundUnboundUnboundUnbound
1ejnA02Unbound UnboundUnboundUnboundUnbound
1f5lA02Unbound UnboundUnboundUnboundUnbound
1f92A02Unbound UnboundUnboundUnboundUnbound
1fv9A02Unbound UnboundUnboundUnboundUnbound
1gi7B02Unbound UnboundUnboundUnboundUnbound
1gi8B02Unbound UnboundUnboundUnboundUnbound
1gi9B02Unbound UnboundUnboundUnboundUnbound
1gj7B02Unbound UnboundUnboundUnboundUnbound
1gj8B02Unbound UnboundUnboundUnboundUnbound
1gj9B02Unbound UnboundUnboundUnboundUnbound
1gjaB02Unbound UnboundUnboundUnboundUnbound
1gjbB02Unbound UnboundUnboundUnboundUnbound
1gjcB02Unbound UnboundUnboundUnboundUnbound
1gjdB02Unbound UnboundUnboundUnboundUnbound
1lmwB02Unbound UnboundUnboundUnboundUnbound
1lmwD02Unbound UnboundUnboundUnboundUnbound
1o3pB02Unbound UnboundUnboundUnboundUnbound
1owdA02Unbound UnboundUnboundUnboundUnbound
1oweA02Unbound UnboundUnboundUnboundUnbound
1owhA02Unbound UnboundUnboundUnboundUnbound
1owiA02Unbound UnboundUnboundUnboundUnbound
1owjA02Unbound UnboundUnboundUnboundUnbound
1owkA02Unbound UnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesMain-chain involved in catalysis
          
1urkA01 
 
1urkA02 
 
1kduA 
 
1c5wB01SER 195
GLY 193;SER 195
1c5xB01SER 195
GLY 193;SER 195
1c5yB01SER 195
GLY 193;SER 195
1c5zB01SER 195
GLY 193;SER 195
1ejnA01SER 195
GLY 193;SER 195
1f5lA01SER 195
GLY 193;SER 195
1f92A01SER 195
GLY 193;SER 195
1fv9A01SER 197
GLY 193;SER 195
1gi7B01SER 195
GLY 193;SER 195
1gi8B01SER 195
GLY 193;SER 195
1gi9B01SER 195
GLY 193;SER 195
1gj7B01SER 195
GLY 193;SER 195
1gj8B01SER 195
GLY 193;SER 195
1gj9B01SER 195
GLY 193;SER 195
1gjaB01SER 195
GLY 193;SER 195
1gjbB01SER 195
GLY 193;SER 195
1gjcB01SER 195
GLY 193;SER 195
1gjdB01SER 195
GLY 193;SER 195
1lmwB01SER 195
GLY 193;SER 195
1lmwD01SER 195
GLY 193;SER 195
1o3pB01SER 195
GLY 193;SER 195
1owdA01SER 197
GLY 193;SER 195
1oweA01SER 211
GLY 193;SER 195
1owhA01SER 211
GLY 193;SER 195
1owiA01SER 197
GLY 193;SER 195
1owjA01SER 197
GLY 193;SER 195
1owkA01SER 197
GLY 193;SER 195
1c5wB02HIS 57;ASP 102
 
1c5xB02HIS 57;ASP 102
 
1c5yB02HIS 57;ASP 102
 
1c5zB02HIS 57;ASP 102
 
1ejnA02HIS 57;ASP 102
 
1f5lA02HIS 57;ASP 102
 
1f92A02HIS 57;ASP 102
 
1fv9A02HIS 45;ASP  96
 
1gi7B02HIS 57;ASP 102
 
1gi8B02HIS 57;ASP 102
 
1gi9B02HIS 57;ASP 102
 
1gj7B02HIS 57;ASP 102
 
1gj8B02HIS 57;ASP 102
 
1gj9B02HIS 57;ASP 102
 
1gjaB02HIS 57;ASP 102
 
1gjbB02HIS 57;ASP 102
 
1gjcB02HIS 57;ASP 102
 
1gjdB02HIS 57;ASP 102
 
1lmwB02HIS 57;ASP 102
 
1lmwD02HIS 57;ASP 102
 
1o3pB02HIS 57;ASP 102
 
1owdA02HIS 45;ASP  96
 
1oweA02HIS 54;ASP 109
 
1owhA02HIS 54;ASP 109
 
1owiA02HIS 45;ASP  96
 
1owjA02HIS 45;ASP  96
 
1owkA02HIS 45;ASP  96
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[19]

[45]


references
[1]
PubMed ID6498202
JournalBiochim Biophys Acta
Year1984
Volume791
Pages1-8
AuthorsMiwa N, Sawada T, Suzuki A
TitleConformational changes in human urokinase induced by a specific reduction of disulfide bond in Cys-194-Cys-222 associated with exhibition of enzymatic activity.
[2]
PubMed ID3114883
JournalSemin Thromb Hemost
Year1987
Volume13
Pages152-9
AuthorsLijnen HR, Stump DC, Collen DC
TitleSingle-chain urokinase-type plasminogen activator: mechanism of action and thrombolytic properties.
[3]
PubMed ID3365258
JournalBiochem Biophys Res Commun
Year1988
Volume152
Pages910-5
AuthorsCharpie JR, Haber E, Matsueda GR
TitleA sequence-dependent monoclonal antibody specific for single-chain urokinase.
[4]
PubMed ID2894309
JournalEur J Biochem
Year1988
Volume172
Pages185-8
AuthorsLijnen HR, Van Hoef B, Nelles L, Holmes WE, Collen D
TitleEnzymatic properties of single-chain and two-chain forms of a Lys158----Glu158 mutant of urokinase-type plasminogen activator.
[5]
CommentsSTRUCTURE BY NMR.
Medline ID89127526
PubMed ID2536903
JournalNature
Year1989
Volume337
Pages579-82
AuthorsOswald RE, Bogusky MJ, Bamberger M, Smith RA, Dobson CM
TitleDynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR.
Related UniProtKBP00749
[6]
PubMed ID1847867
JournalEur J Biochem
Year1991
Volume195
Pages691-7
AuthorsOrsini G, Brandazza A, Sarmientos P, Molinari A, Lansen J, Cauet G
TitleEfficient renaturation and fibrinolytic properties of prourokinase and a deletion mutant expressed in Escherichia coli as inclusion bodies.
[7]
CommentsSTRUCTURE BY NMR OF 67-155.
Medline ID93003110
PubMed ID1327118
JournalBiochemistry
Year1992
Volume31
Pages9562-71
AuthorsLi X, Smith RA, Dobson CM
TitleSequential 1H NMR assignments and secondary structure of the kringle domain from urokinase.
Related PDB1kdu
Related UniProtKBP00749
[8]
PubMed ID1510944
JournalBiochemistry
Year1992
Volume31
Pages7572-9
AuthorsStephens RW, Bokman AM, Myohanen HT, Reisberg T, Tapiovaara H, Pedersen N, Grondahl-Hansen J, Llinas M, Vaheri A
TitleHeparin binding to the urokinase kringle domain.
[9]
PubMed ID1310986
JournalJ Biol Chem
Year1992
Volume267
Pages3878-85
AuthorsNovokhatny V, Medved L, Mazar A, Marcotte P, Henkin J, Ingham K
TitleDomain structure and interactions of recombinant urokinase-type plasminogen activator.
[10]
PubMed ID8380336
JournalBiochemistry
Year1993
Volume32
Pages298-309
AuthorsNowak UK, Li X, Teuten AJ, Smith RA, Dobson CM
TitleNMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator.
[11]
PubMed ID8314753
JournalJ Biol Chem
Year1993
Volume268
Pages13858-68
AuthorsBokman AM, Jimenez-Barbero J, Llinas M
Title1H NMR characterization of the urokinase kringle module. Structural, but not functional, relatedness to homologous domains.
[12]
PubMed ID8449917
JournalJ Biol Chem
Year1993
Volume268
Pages5550-6
AuthorsLubin IM, Caban R, Runge MS
TitleThe tissue plasminogen activator finger domain confers fibrin-dependent enhancement of catalytic activity to single-chain urokinase-type plasminogen activator.
[13]
PubMed ID7803405
JournalBiochemistry
Year1994
Volume33
Pages15418-24
AuthorsHansen AP, Petros AM, Meadows RP, Fesik SW
TitleBackbone dynamics of a two-domain protein: 15N relaxation studies of the amino-terminal fragment of urokinase-type plasminogen activator.
[14]
CommentsX-ray crystallography
PubMed ID8161544
JournalBiochemistry
Year1994
Volume33
Pages4847-64
AuthorsHansen AP, Petros AM, Meadows RP, Nettesheim DG, Mazar AP, Olejniczak ET, Xu RX, Pederson TM, Henkin J, Fesik SW
TitleSolution structure of the amino-terminal fragment of urokinase-type plasminogen activator.
Related PDB1urk
[15]
PubMed ID8130209
JournalBiochemistry
Year1994
Volume33
Pages2951-60
AuthorsNowak UK, Cooper A, Saunders D, Smith RA, Dobson CM
TitleUnfolding studies of the protease domain of urokinase-type plasminogen activator: the existence of partly folded states and stable subdomains.
[16]
CommentsSTRUCTURE BY NMR OF 67-155.
Medline ID94149701
PubMed ID8107091
JournalJ Mol Biol
Year1994
Volume235
Pages1548-59
AuthorsLi X, Bokman AM, Llinas M, Smith RA, Dobson CM
TitleSolution structure of the kringle domain from urokinase-type plasminogen activator.
Related UniProtKBP00749
[17]
PubMed ID7548000
JournalBiochemistry
Year1995
Volume34
Pages12524-34
AuthorsPloug M, Rahbek-Nielsen H, Ellis V, Roepstorff P, Dano K
TitleChemical modification of the urokinase-type plasminogen activator and its receptor using tetranitromethane. Evidence for the involvement of specific tyrosine residues in both molecules during receptor-ligand interaction.
[18]
PubMed ID8869642
JournalProtein Eng
Year1995
Volume8
Pages1295-1302
AuthorsBakker AH, Nieuwenbroek NM, Verheijen JH
TitleDomain-domain interactions in hybrids of tissue-type plasminogen activator and urokinase-type plasminogen activator.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID96000858
PubMed ID8591045
JournalStructure
Year1995
Volume3
Pages681-91
AuthorsSpraggon G, Phillips C, Nowak UK, Ponting CP, Saunders D, Dobson CM, Stuart DI, Jones EY
TitleThe crystal structure of the catalytic domain of human urokinase-type plasminogen activator.
Related PDB1lmw
Related UniProtKBP00749
[20]
PubMed ID8647121
JournalEur J Biochem
Year1996
Volume237
Pages743-51
AuthorsMagdolen V, Rettenberger P, Koppitz M, Goretzki L, Kessler H, Weidle UH, Konig B, Graeff H, Schmitt M, Wilhelm O
TitleSystematic mutational analysis of the receptor-binding region of the human urokinase-type plasminogen activator.
[21]
PubMed ID9295329
JournalJ Biol Chem
Year1997
Volume272
Pages23818-23
AuthorsSun Z, Jiang Y, Ma Z, Wu H, Liu BF, Xue Y, Tang W, Chen Y, Li C, Zhu D, Gurewich V, Liu JN, Zhong M, Xu Y
TitleIdentification of a flexible loop region (297-313) of urokinase-type plasminogen activator, which helps determine its catalytic activity.
[22]
PubMed ID9843416
JournalBiochemistry
Year1998
Volume37
Pages16494-505
AuthorsPloug M
TitleIdentification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site.
[23]
PubMed ID9521680
JournalBiochemistry
Year1998
Volume37
Pages3612-22
AuthorsPloug M, Ostergaard S, Hansen LB, Holm A, Dano K
TitlePhotoaffinity labeling of the human receptor for urokinase-type plasminogen activator using a decapeptide antagonist. Evidence for a composite ligand-binding site and a short interdomain separation.
[24]
PubMed ID9485445
JournalBiochemistry
Year1998
Volume37
Pages2935-40
AuthorsSun Z, Liu BF, Chen Y, Gurewich V, Zhu D, Liu JN
TitleAnalysis of the forces which stabilize the active conformation of urokinase-type plasminogen activator.
[25]
PubMed ID9804393
JournalClin Chem Lab Med
Year1998
Volume36
Pages697-702
AuthorsOrgel D, Schroder W, Hecker-Kia A, Weithmann KU, Kolkenbrock H, Ulbrich N
TitleThe cleavage of pro-urokinase type plasminogen activator by stromelysin-1.
[26]
PubMed ID9760182
JournalEur J Biochem
Year1998
Volume256
Pages411-8
AuthorsOda M, Shiraishi A, Hasegawa M
TitleAnalysis of the ternary complex formation of human urokinase with the separated two domains of its receptor.
[27]
PubMed ID10540331
JournalEur J Immunol
Year1999
Volume29
Pages3196-209
AuthorsOlivier P, Bieler G, Muller KM, Hauzenberger D, Ruegg C
TitleUrokinase-type plasminogen activator inhibits alpha 4 beta 1 integrin-mediated T lymphocyte adhesion to fibronectin independently of its catalytic activity.
[28]
CommentsX-ray crystallography
PubMed ID10779411
JournalChem Biol
Year2000
Volume7
Pages299-312
AuthorsKatz BA, Mackman R, Luong C, Radika K, Martelli A, Sprengeler PA, Wang J, Chan H, Wong L
TitleStructural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator.
Related PDB1c5w,1c5x,1c5y,1c5z
[29]
CommentsX-ray crystallography
PubMed ID10926521
JournalJ Mol Biol
Year2000
Volume301
Pages465-75
AuthorsZeslawska E, Schweinitz A, Karcher A, Sondermann P, Sperl S, Sturzebecher J, Jacob U
TitleCrystals of the urokinase type plasminogen activator variant beta(c)-uPAin complex with small molecule inhibitors open the way towards structure-based drug design.
Related PDB1f5l,1f92
[30]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
Medline ID20266327
PubMed ID10805774
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages5113-8
AuthorsSperl S, Jacob U, Arroyo de Prada N, Sturzebecher J, Wilhelm OG, Bode W, Magdolen V, Huber R, Moroder L
Title(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase.
Related PDB1ejn
Related UniProtKBP00749
[31]
PubMed ID11150590
JournalThromb Res
Year2000
Volume100
Pages461-7
AuthorsWang P, Zhang J, Sun Z, Chen Y, Gurewich V, Liu JN
TitleCatalytic and fibrinolytic properties of recombinant urokinase plasminogen activator from E. coli, mammalian, and yeast cells.
[32]
CommentsX-ray crystallography
PubMed ID11731301
JournalChem Biol
Year2001
Volume8
Pages1107-21
AuthorsKatz BA, Sprengeler PA, Luong C, Verner E, Elrod K, Kirtley M, Janc J, Spencer JR, Breitenbucher JG, Hui H, McGee D, Allen D, Martelli A, Mackman RL
TitleEngineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets.
Related PDB1gj7,1gj8,1gj9,1gja,1gjb,1gjc,1gjd
[33]
PubMed ID11562773
JournalInt J Mol Med
Year2001
Volume8
Pages365-71
AuthorsJankun J, Skrzypczak-Jankun E
TitleBinding site of amiloride to urokinase plasminogen activator depends on species.
[34]
PubMed ID11689072
JournalJ Med Chem
Year2001
Volume44
Pages3856-71
AuthorsMackman RL, Katz BA, Breitenbucher JG, Hui HC, Verner E, Luong C, Liu L, Sprengeler PA
TitleExploiting subsite S1 of trypsin-like serine proteases for selectivity: potent and selective inhibitors of urokinase-type plasminogen activator.
[35]
PubMed ID11495587
JournalJ Med Chem
Year2001
Volume44
Pages2753-71
AuthorsVerner E, Katz BA, Spencer JR, Allen D, Hataye J, Hruzewicz W, Hui HC, Kolesnikov A, Li Y, Luong C, Martelli A, Radika K, Rai R, She M, Shrader W, Sprengeler PA, Trapp S, Wang J, Young WB, Mackman RL
TitleDevelopment of serine protease inhibitors displaying a multicentered short (<2.3 A) hydrogen bond binding mode: inhibitors of urokinase-type plasminogen activator and factor Xa.
[36]
CommentsX-ray crystallography
PubMed ID11292354
JournalJ Mol Biol
Year2001
Volume307
Pages1451-86
AuthorsKatz BA, Elrod K, Luong C, Rice MJ, Mackman RL, Sprengeler PA, Spencer J, Hataye J, Janc J, Link J, Litvak J, Rai R, Rice K, Sideris S, Verner E, Young W
TitleA novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site.
Related PDB1gi7,1gi8,1gi9
[37]
PubMed ID11841346
JournalBiochemistry (Mosc)
Year2002
Volume67
Pages109-18
AuthorsStepanova VV, Tkachuk VA
TitleUrokinase as a multidomain protein and polyfunctional cell regulator.
[38]
PubMed ID12113832
JournalBioorg Med Chem Lett
Year2002
Volume12
Pages2019-22
AuthorsMackman RL, Hui HC, Breitenbucher JG, Katz BA, Luong C, Martelli A, McGee D, Radika K, Sendzik M, Spencer JR, Sprengeler PA, Tario J, Verner E, Wang J
Title2-(2-Hydroxy-3-alkoxyphenyl)-1H-benzimidazole-5-carboxamidine derivatives as potent and selective urokinase-type plasminogen activator inhibitors.
[39]
PubMed ID12113833
JournalBioorg Med Chem Lett
Year2002
Volume12
Pages2023-6
AuthorsSpencer JR, McGee D, Allen D, Katz BA, Luong C, Sendzik M, Squires N, Mackman RL
Title4-Aminoarylguanidine and 4-aminobenzamidine derivatives as potent and selective urokinase-type plasminogen activator inhibitors.
[40]
PubMed ID12369939
JournalCurr Pharm Des
Year2002
Volume8
Pages2541-58
AuthorsRockway TW, Nienaber V, Giranda VL
TitleInhibitors of the protease domain of urokinase-type plasminogen activator.
[41]
PubMed ID12408709
JournalJ Med Chem
Year2002
Volume45
Pages4984-94
AuthorsSchmiedeberg N, Schmitt M, Rolz C, Truffault V, Sukopp M, Burgle M, Wilhelm OG, Schmalix W, Magdolen V, Kessler H
TitleSynthesis, solution structure, and biological evaluation of urokinase type plasminogen activator (uPA)-derived receptor binding domain mimetics.
[42]
PubMed ID12182908
JournalThromb Res
Year2002
Volume106
Pages105-11
AuthorsSun Z, Zhang PX, Wang P, Gurewich V, Shen HY, Liu JN
TitleAmino-terminal fragment of urokinase-type plasminogen activator inhibits its plasminogen activation.
[43]
PubMed ID12675515
JournalBiol Chem
Year2003
Volume384
Pages229-36
AuthorsLiang OD, Chavakis T, Linder M, Bdeir K, Kuo A, Preissner KT
TitleBinding of urokinase plasminogen activator to gp130 via a putative urokinase-binding consensus sequence.
[44]
PubMed ID12529357
JournalJ Biol Chem
Year2003
Volume278
Pages11449-56
AuthorsKim KS, Hong YK, Joe YA, Lee Y, Shin JY, Park HE, Lee IH, Lee SY, Kang DK, Chang SI, Chung SI
TitleAnti-angiogenic activity of the recombinant kringle domain of urokinase and its specific entry into endothelial cells.
[45]
CommentsX-ray crystallography
PubMed ID12742021
JournalJ Mol Biol
Year2003
Volume329
Pages93-120
AuthorsKatz BA, Elrod K, Verner E, Mackman RL, Luong C, Shrader WD, Sendzik M, Spencer JR, Sprengeler PA, Kolesnikov A, Tai VW, Hui HC, Breitenbucher JG, Allen D, Janc JW
TitleElaborate manifold of short hydrogen bond arrays mediating binding of active site-directed serine protease inhibitors.
Related PDB1o3p
[46]
PubMed ID12684001
JournalJ Mol Biol
Year2003
Volume328
Pages109-18
AuthorsZeslawska E, Jacob U, Schweinitz A, Coombs G, Bode W, Madison E
TitleCrystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors.
[47]
CommentsX-ray crystallography
PubMed ID14711304
JournalJ Med Chem
Year2004
Volume47
Pages303-24
AuthorsWendt MD, Rockway TW, Geyer A, McClellan W, Weitzberg M, Zhao X, Mantei R, Nienaber VL, Stewart K, Klinghofer V, Giranda VL
TitleIdentification of novel binding interactions in the development of potent, selective 2-naphthamidine inhibitors of urokinase. Synthesis, structural analysis, and SAR of N-phenyl amide 6-substitution.
Related PDB1owd,1owe,1owh,1owi,1owj,1owk

comments
This enzyme is composed of the N-terminal EGF-like domain (corresponding to 1urk), Kringle one (corresponding to 1urk & 1kdu) and serine protease ones. This enzyme belongst to the peptidase family-S1. It has a classic catalytic triad (ser/His/Asp), suggesting that it has a similar catalytic mechanism to that of other serine proteases, such as trypsin (D00197 in EzCatDB).

createdupdated
2004-11-092011-02-21


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