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@article{Bickel:2021:10.1007/978-3-030-58971-4_7,
author = {Bickel, JK and Voisin, TB and Tate, EW and Bubeck, D},
doi = {10.1007/978-3-030-58971-4_7},
journal = {Subcell Biochem},
pages = {273--295},
title = {How Structures of Complement Complexes Guide Therapeutic Design.},
url = {http://dx.doi.org/10.1007/978-3-030-58971-4_7},
volume = {96},
year = {2021}
}
TY - JOUR
AB - The complement system is essential for immune defence against infection and modulation of proinflammatory responses. Activation of the terminal pathway of complement triggers formation of the membrane attack complex (MAC), a multi-protein pore that punctures membranes. Recent advances in structural biology, specifically cryo-electron microscopy (cryoEM), have provided atomic resolution snapshots along the pore formation pathway. These structures have revealed dramatic conformational rearrangements that enable assembly and membrane rupture. Here we review the structural basis for MAC formation and show how soluble proteins transition into a giant β-barrel pore. We also discuss regulatory complexes of the terminal pathway and their impact on structure-guided drug discovery of complement therapeutics.
AU - Bickel,JK
AU - Voisin,TB
AU - Tate,EW
AU - Bubeck,D
DO - 10.1007/978-3-030-58971-4_7
EP - 295
PY - 2021///
SN - 0306-0225
SP - 273
TI - How Structures of Complement Complexes Guide Therapeutic Design.
T2 - Subcell Biochem
UR - http://dx.doi.org/10.1007/978-3-030-58971-4_7
UR - https://www.ncbi.nlm.nih.gov/pubmed/33252733
VL - 96
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821