3OXU

Complement components factor H CCP19-20 and C3d in complex

3OXU の概要

• エントリーDOI: 10.2210/pdb3oxu/pdb
• 関連するPDBエントリー: 1C3D 2G7I
• 分子名称: Complement C3, HF protein, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: c3d-alpha-alpha barrel, complement component, factor h, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P01024
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 151391.45

構造登録者

Morgan, H.P.,Schmidt, C.Q.,Guariento, M.,Gillespie, D.,Herbert, A.P.,Mertens, H.,Blaum, B.S.,Svergun, D.,Johansson, C.M.,Uhrin, D.,Barlow, P.N.,Hannan, J.P. (登録日: 2010-09-22, 公開日: 2011-02-16, 最終更新日: 2024-10-30)

主引用文献

Morgan, H.P.,Schmidt, C.Q.,Guariento, M.,Blaum, B.S.,Gillespie, D.,Herbert, A.P.,Kavanagh, D.,Mertens, H.D.,Svergun, D.I.,Johansson, C.M.,Uhrin, D.,Barlow, P.N.,Hannan, J.P.
Structural basis for engagement by complement factor H of C3b on a self surface.
Nat.Struct.Mol.Biol., 18:463-470, 2011

PubMed Abstract: Complement factor H (FH) attenuates C3b molecules tethered by their thioester domains to self surfaces and thereby protects host tissues. Factor H is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d) corresponding to the thioester domain. We used NMR and X-ray crystallography to study the C3d-FH19-20 complex in atomic detail and identify glycosaminoglycan-binding residues in factor H module 20 of the C3d-FH19-20 complex. Mutagenesis justified the merging of the C3d-FH19-20 structure with an existing C3b-FH1-4 crystal structure. We concatenated the merged structure with the available FH6-8 crystal structure and new SAXS-derived FH1-4, FH8-15 and FH15-19 envelopes. The combined data are consistent with a bent-back factor H molecule that binds through its termini to two sites on one C3b molecule and simultaneously to adjacent polyanionic host-surface markers.

PubMed: 21317894
DOI: 10.1038/nsmb.2018

実験手法

X-RAY DIFFRACTION (2.1 Å)