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1OJW

Decay accelerating factor (CD55): the structure of an intact human complement regulator.

1OJW の概要
エントリーDOI10.2210/pdb1ojw/pdb
関連するPDBエントリー1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJY 1OK1 1OK2 1OK3 1OK9 1UOT 1UPN
分子名称COMPLEMENT DECAY-ACCELERATING FACTOR, SULFATE ION, GLYCEROL, ... (4 entities in total)
機能のキーワードregulator of complement pathway, regulator of complement, decay acceleration of c3/c5 convertases, pathogen receptor, short consensus repeat domains
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56725.65
構造登録者
主引用文献Lukacik, P.,Roversi, P.,White, J.,Esser, D.,Smith, G.P.,Billington, J.,Williams, P.A.,Rudd, P.M.,Wormald, M.R.,Harvey, D.J.,Crispin, M.D.M.,Radcliffe, C.M.,Dwek, R.A.,Evans, D.J.,Morgan, B.P.,Smith, R.A.G.,Lea, S.M.
Complement Regulation at the Molecular Level: The Structure of Decay-Accelerating Factor
Proc.Natl.Acad.Sci.USA, 101:1279-, 2004
Cited by
PubMed Abstract: The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.
PubMed: 14734808
DOI: 10.1073/PNAS.0307200101
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1ojw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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