1LMW

LMW U-PA Structure complexed with EGRCMK (GLU-GLY-ARG Chloromethyl Ketone)

Summary for 1LMW

• Entry DOI: 10.2210/pdb1lmw/pdb
• Related PRD ID: PRD_000288
• Descriptor: UROKINASE-TYPE PLASMINOGEN ACTIVATOR, L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide (3 entities in total)
• Functional Keywords: fibrinolysis, trypsin-like serine protease, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P00749 P00749
• Total number of polymer chains: 4
• Total formula weight: 63164.99

Authors

Spraggon, G.S.,Phillips, C.,Nowak, U.K.,Ponting, C.P.,Saunders, D.,Dobson, C.M.,Stuart, D.I.,Jones, E.Y. (deposition date: 1995-07-26, release date: 1996-01-29, Last modification date: 2024-10-30)

Primary citation

Spraggon, G.,Phillips, C.,Nowak, U.K.,Ponting, C.P.,Saunders, D.,Dobson, C.M.,Stuart, D.I.,Jones, E.Y.
The crystal structure of the catalytic domain of human urokinase-type plasminogen activator.
Structure, 3:681-691, 1995

PubMed Abstract: Urokinase-type plasminogen activator (u-PA) promotes fibrinolysis by catalyzing the conversion of plasminogen to the active protease plasmin via the cleavage of a peptide bond. When localized to the external cell surface it contributes to tissue remodelling and cellular migration; inhibition of its activity impedes the spread of cancer. u-PA has three domains: an N-terminal receptor-binding growth factor domain, a central kringle domain and a C-terminal catalytic protease domain. The biological roles of the fibrinolytic enzymes render them therapeutic targets, however, until now no structure of the protease domain has been available. Solution of the structure of the u-PA serine protease was undertaken to provide such data.

PubMed: 8591045
DOI: 10.1016/S0969-2126(01)00203-9

Experimental method

X-RAY DIFFRACTION (2.5 Å)