6RMT

Crystal structure of disulphide-linked human C3d dimer

6RMT の概要

• エントリーDOI: 10.2210/pdb6rmt/pdb
• 分子名称: Complement C3, CHLORIDE ION (3 entities in total)
• 機能のキーワード: complement, innate immunity, immune system
• 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: 69699.44

構造登録者

Wahid, A.A.,van den Elsen, J.M.H.,Crennell, S.J. (登録日: 2019-05-07, 公開日: 2020-11-18, 最終更新日: 2024-10-16)

主引用文献

Wahid, A.A.,Dunphy, R.W.,Macpherson, A.,Gibson, B.G.,Kulik, L.,Whale, K.,Back, C.,Hallam, T.M.,Alkhawaja, B.,Martin, R.L.,Meschede, I.,Laabei, M.,Lawson, A.D.G.,Holers, V.M.,Watts, A.G.,Crennell, S.J.,Harris, C.L.,Marchbank, K.J.,van den Elsen, J.M.H.
Insights Into the Structure-Function Relationships of Dimeric C3d Fragments.
Front Immunol, 12:714055-714055, 2021

PubMed Abstract: Cleavage of C3 to C3a and C3b plays a central role in the generation of complement-mediated defences. Although the thioester-mediated surface deposition of C3b has been well-studied, fluid phase dimers of C3 fragments remain largely unexplored. Here we show C3 cleavage results in the spontaneous formation of C3b dimers and present the first X-ray crystal structure of a disulphide-linked human C3d dimer. Binding studies reveal these dimers are capable of crosslinking complement receptor 2 and preliminary cell-based analyses suggest they could modulate B cell activation to influence tolerogenic pathways. Altogether, insights into the physiologically-relevant functions of C3d(g) dimers gained from our findings will pave the way to enhancing our understanding surrounding the importance of complement in the fluid phase and could inform the design of novel therapies for immune system disorders in the future.

PubMed: 34434196
DOI: 10.3389/fimmu.2021.714055

実験手法

X-RAY DIFFRACTION (2 Å)