1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7

Authors:	Marie M. Phelan Chuong-Thu Thai Andrew P. Herbert Juraj Bella Dušan Uhrín Ronald T. Ogata Paul N. Barlow Janice Bramham

Affiliation:	(1) Edinburgh Biomolecular NMR Unit, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, Scotland, UK;(2) Torrey Pines Institute for Molecular Studies, 3550 General Atomics Court, San Diego, USA

Abstract:	The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the ¹H, ¹⁵N and ¹³C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.

Keywords:	Complement Membrane attack complex MAC C7 Factor I module FIM NMR Resonance assignment
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