1DST

MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY

1DST の概要

• エントリーDOI: 10.2210/pdb1dst/pdb
• 分子名称: FACTOR D (2 entities in total)
• 機能のキーワード: complement activating enzyme, hydrolase, serine protease, factor d, hydrolase (serine protease)
• 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: 1
• 化学式量合計: 24600.01

構造登録者

Narayana, S.V.L.,Volanakis, J.E. (登録日: 1995-09-13, 公開日: 1996-07-11, 最終更新日: 2024-10-16)

主引用文献

Kim, S.,Narayana, S.V.,Volanakis, J.E.
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.
J.Biol.Chem., 270:24399-24405, 1995

PubMed Abstract: Complement factor D is a serine protease regulated by a novel mechanism that depends on conformational changes rather than cleavage of a zymogen for expression of proteolytic activity. The conformational changes are presumed to be induced by the single natural substrate, C3bB, and to result in reversible reorientation of the catalytic center and of the substrate binding site of factor D, both of which have atypical conformations. Here we report that replacement of Ser94, Thr214, and Ser215 of factor D (chymotrypsinogen numbering has been used for comparison purposes) with the corresponding residues of trypsin, Tyr, Ser, and Trp, is sufficient to induce substantially higher catalytic activity associated with a typical serine protease alignment of the catalytic triad residues His57, Asp102, and Ser195. These results provide a partial structural explanation for the low reactivity of "resting-state" factor D toward synthetic substrates.

PubMed: 7592653
DOI: 10.1074/jbc.270.41.24399

実験手法

X-RAY DIFFRACTION (2 Å)