4DUR

The X-ray Crystal Structure of Full-Length type II Human Plasminogen

4DUR の概要

• エントリーDOI: 10.2210/pdb4dur/pdb
• 関連するPDBエントリー: 4DUU
• 分子名称: Plasminogen, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: serine protease, fibrinolysis, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 178945.58

構造登録者

Law, R.H.P.,Caradoc-Davies, T.,Whisstock, J.C. (登録日: 2012-02-22, 公開日: 2012-03-28, 最終更新日: 2024-10-09)

主引用文献

Law, R.H.P.,Caradoc-Davies, T.,Cowieson, N.,Horvath, A.J.,Quek, A.J.,Encarnacao, J.A.,Steer, D.,Cowan, A.,Zhang, Q.,Lu, B.G.C.,Pike, R.N.,Smith, A.I.,Coughlin, P.B.,Whisstock, J.C.
The X-ray crystal structure of full-length human plasminogen
Cell Rep, 1:185-190, 2012

PubMed Abstract: Plasminogen is the proenzyme precursor of the primary fibrinolytic protease plasmin. Circulating plasminogen, which comprises a Pan-apple (PAp) domain, five kringle domains (KR1-5), and a serine protease (SP) domain, adopts a closed, activation-resistant conformation. The kringle domains mediate interactions with fibrin clots and cell-surface receptors. These interactions trigger plasminogen to adopt an open form that can be cleaved and converted to plasmin by tissue-type and urokinase-type plasminogen activators. Here, the structure of closed plasminogen reveals that the PAp and SP domains, together with chloride ions, maintain the closed conformation through interactions with the kringle array. Differences in glycosylation alter the position of KR3, although in all structures the loop cleaved by plasminogen activators is inaccessible. The ligand-binding site of KR1 is exposed and likely governs proenzyme recruitment to targets. Furthermore, analysis of our structure suggests that KR5 peeling away from the PAp domain may initiate plasminogen conformational change.

PubMed: 22832192
DOI: 10.1016/j.celrep.2012.02.012

実験手法

X-RAY DIFFRACTION (2.45 Å)