| Literature DB >> 27391278 |
Hongyu Yuan1, Rong Chen1, Mansoor Tariq1, Yanjie Liu1, Yaping Sun1, Chun Xia2,3.
Abstract
C1q contains three globular domains (C1qgD) that are the key functional component of the classical complement system. C1qgD can interact with important immune molecules, including IgG and C-reactive protein (CRP) to form defense systems to protect animals. Here, the first non-mammalian structure, zebrafish C1qA globular domain (Dare-C1qAgD) was solved. Although the overall architecture of Dare-C1qAgD is similar to human C1qA, residues involved in C1qBgD, C1qCgD, and CRP binding are somewhat different while residues involved in IgG binding are not present in zebrafish. The structure gives insight into how human and fish C1qA evolved from an ancestral protein.Entities:
Keywords: C1q globular domain; evolution; structure; zebrafish
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Year: 2016 PMID: 27391278 PMCID: PMC5029524 DOI: 10.1002/pro.2980
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725