2XWA

Crystal Structure of Complement Factor D Mutant R202A

2XWA の概要

• エントリーDOI: 10.2210/pdb2xwa/pdb
• 関連するPDBエントリー: 1BIO 1DFP 1DIC 1DST 1DSU 1FDP 1HFD 2XW9 2XWB 2XWJ
• 分子名称: COMPLEMENT FACTOR D, GLYCEROL (3 entities in total)
• 機能のキーワード: immune system, hydrolase, serine protease, alternative pathway
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Secreted: P00746
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48889.57

構造登録者

Forneris, F.,Ricklin, D.,Wu, J.,Tzekou, A.,Wallace, R.S.,Lambris, J.D.,Gros, P. (登録日: 2010-11-01, 公開日: 2011-01-12, 最終更新日: 2024-11-13)

主引用文献

Forneris, F.,Ricklin, D.,Wu, J.,Tzekou, A.,Wallace, R.S.,Lambris, J.D.,Gros, P.
Structures of C3B in Complex with Factors B and D Give Insight Into Complement Convertase Formation.
Science, 330:1816-, 2010

PubMed Abstract: Activation of the complement cascade induces inflammatory responses and marks cells for immune clearance. In the central complement-amplification step, a complex consisting of surface-bound C3b and factor B is cleaved by factor D to generate active convertases on targeted surfaces. We present crystal structures of the pro-convertase C3bB at 4 angstrom resolution and its complex with factor D at 3.5 angstrom resolution. Our data show how factor B binding to C3b forms an open "activation" state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D's self-inhibitory loop. This concerted proteolytic mechanism, which is cofactor-dependent and substrate-induced, restricts complement amplification to C3b-tagged target cells.

PubMed: 21205667
DOI: 10.1126/SCIENCE.1195821

実験手法

X-RAY DIFFRACTION (2.8 Å)