1DLE

FACTOR B SERINE PROTEASE DOMAIN

1DLE の概要

• エントリーDOI: 10.2210/pdb1dle/pdb
• 分子名称: COMPLEMENT FACTOR B (2 entities in total)
• 機能のキーワード: serine protease, complement system, factor b, protein-protein interaction, activation mechanism, beta-barrel fold, 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: 67397.12

構造登録者

Jing, H.,Xu, Y.,Carson, M.,Moore, D.,Macon, K.J.,Volanakis, J.E.,Narayana, S.V. (登録日: 1999-12-09, 公開日: 2000-12-13, 最終更新日: 2024-11-06)

主引用文献

Jing, H.,Xu, Y.,Carson, M.,Moore, D.,Macon, K.J.,Volanakis, J.E.,Narayana, S.V.
New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.
EMBO J., 19:164-173, 2000

PubMed Abstract: Factor B and C2 are two central enzymes for complement activation. They are multidomain serine proteases and require cofactor binding for full expression of proteolytic activities. We present a 2.1 A crystal structure of the serine protease domain of factor B. It shows a number of structural motifs novel to the chymotrypsin fold, which by sequence homology are probably present in C2 as well. These motifs distribute characteristically on the protein surface. Six loops surround the active site, four of which shape substrate-binding pockets. Three loops next to the oxyanion hole, which typically mediate zymogen activation, are much shorter or absent. Three insertions including the linker to the preceding domain bulge from the side opposite to the active site. The catalytic triad and non-specific substrate-binding site display active conformations, but the oxyanion hole displays a zymogen-like conformation. The bottom of the S1 pocket has a negative charge at residue 226 instead of the typical 189 position. These unique structural features may play different roles in domain-domain interaction, cofactor binding and substrate binding.

PubMed: 10637221
DOI: 10.1093/emboj/19.2.164

実験手法

X-RAY DIFFRACTION (2.1 Å)