C1q and its growing family

被引：164

作者：

Ghai, Rohit

Waters, Patrick

Roumenina, Lubka T.

Gadjeva, Mihaela

Kojouharova, Mihaela S.

Reid, Kenneth B. M.

Sim, Robert B.

Kishore, Uday ^{[1
]}

机构：

[1] Brunel Univ, Sch Hlth Sci & Social Care, Lab Human Immunol, Uxbridge UB8 3PH, Middx, England

[2] Univ Oxford, Dept Biochem, MRC, Immunochem Unit, Oxford OX1 3QU, England

[3] Harvard Univ, Sch Med, Brigham & Womens Hosp, Dept Pathol, Boston, MA 02115 USA

[4] Univ Sofia, Dept Biochem, BU-1164 Sofia, Bulgaria

[5] Univ Oxford, John Radcliffe Hosp, Weatherall Inst Mol Med, Oxford OX3 9DS, England

[6] Univ Giessen, Inst Med Microbiol, D-35392 Giessen, Germany

来源：

IMMUNOBIOLOGY | 2007年 / 212卷 / 4-5期

关键词：

complement; C1q; module; globular domain; immunity; evolution;

D O I：

10.1016/j.imbio.2006.11.001

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Clq is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, Clq can engage a broad range of self and non-self ligands via its heterotrimeric globular (gClq) domain and thus trigger the classical pathway. The trimeric gClq signature domain has been identified in a variety of non-complement proteins that can be grouped together as a Clq family. The X-ray crystal structures of the gClq domain of a few members of the Clq family reveal a compact jelly-roll P-sandwich fold similar to that of the multifunctional tumor necrosis factor (TNF) ligand family, hence the Clq and TNF superfamily. This review is an update on the structural and functional aspects of the gClq domain of human Clq. We also mention the diverse range of proteins that utilize a gClq domain in order to reflect on its importance as a versatile scaffold to support a variety of functions. (c) 2006 Elsevier GmbH. All rights reserved.

引用

页码：253 / 266

页数：14

共 52 条

[41] Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: Mutational studies using recombinant globular head modules of human C1q A, B, and C chains [J].