1LMW

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

1LMW の概要

• エントリーDOI: 10.2210/pdb1lmw/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000288
• 分子名称: 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)
• 機能のキーワード: fibrinolysis, trypsin-like serine protease, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P00749 P00749
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63164.99

構造登録者

Spraggon, G.S.,Phillips, C.,Nowak, U.K.,Ponting, C.P.,Saunders, D.,Dobson, C.M.,Stuart, D.I.,Jones, E.Y. (登録日: 1995-07-26, 公開日: 1996-01-29, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)