دورية أكاديمية
أعرض في EDS

How Structures of Complement Complexes Guide Therapeutic Design.

التفاصيل البيبلوغرافية
العنوان: How Structures of Complement Complexes Guide Therapeutic Design.
المؤلفون: Bickel JK; Department of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK.; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK., Voisin TB; Department of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK., Tate EW; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK., Bubeck D; Department of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK. d.bubeck@imperial.ac.uk.
المصدر: Sub-cellular biochemistry [Subcell Biochem] 2021; Vol. 96, pp. 273-295.
نوع المنشور: Journal Article; Review
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: United States NLM ID: 0316571 Publication Model: Print Cited Medium: Print ISSN: 0306-0225 (Print) Linking ISSN: 03060225 NLM ISO Abbreviation: Subcell Biochem Subsets: MEDLINE
أسماء مطبوعة: Publication: <2006- > : New York : Springer
Original Publication: London, New York, Plenum Press.
مواضيع طبية MeSH: Drug Design*, Complement Membrane Attack Complex/*chemistry , Complement Membrane Attack Complex/*ultrastructure, Cryoelectron Microscopy ; Humans
مستخلص: 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.
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فهرسة مساهمة: Keywords: C5; Complement therapeutics; Cryo electron microscopy; MACPF; Membrane attack complex; Structure-guided drug discovery
المشرفين على المادة: 0 (Complement Membrane Attack Complex)
تواريخ الأحداث: Date Created: 20201130 Date Completed: 20210210 Latest Revision: 20210922
رمز التحديث: 20240628
DOI: 10.1007/978-3-030-58971-4_7
PMID: 33252733
قاعدة البيانات: MEDLINE
الوصف
تدمد:0306-0225
DOI:10.1007/978-3-030-58971-4_7