Journal article

Publication year: 2004

Pages: 113-128

Journal: Immunology Letters

Volume number: 95

Issue number: 2

ISSN: 0165-2478

eISSN: 1879-0542

Open access status: Green

DOI Link: https://doi.org/10.1016/j.imlet.2004.06.015

Publisher: Elsevier

Abstract: 
Clq is the first subcomponent of the classical pathway of the complement system and a major connecting link between innate and acquired immunity. As a versatile charge pattern recognition molecule, Clq is capable of engaging a broad range of ligands via its heterotrimeric globular domain (gClq) which is composed of the C-terminal regions of its A (ghA), B (ghB) and C (ghQ chains. Recent studies using recombinant forms of ghA, ghB and ghC have suggested that the gClq domain has a modular organization and each chain can have differential ligand specificity. The crystal structure of the gClq, molecular modeling and protein engineering studies have combined to illustrate how modular organization, charge distribution and the spatial orientation of the heterotrimeric assembly offer versatility of ligand recognition to Clq. Although the biochemical and structural studies have provided novel insights into the structure-function relationships within the gClq domain, they have also raised many unexpected issues for debate. (C) 2004 Elsevier B.V. All rights reserved.

Harvard Citation style: Kishore, W., Ghai, R., Greenhough, T., Shrive, A., Bonifati, D., Gadjeva, M., et al. (2004) Structural and functional anatomy of the globular domain of complement protein C1q, Immunology Letters, 95(2), pp. 113-128. https://doi.org/10.1016/j.imlet.2004.06.015

APA Citation style: Kishore, W., Ghai, R., Greenhough, T., Shrive, A., Bonifati, D., Gadjeva, M., Waters, P., Kojouharova, M., Chakraborty, T., & Agrawal, A. (2004). Structural and functional anatomy of the globular domain of complement protein C1q. Immunology Letters. 95(2), 113-128. https://doi.org/10.1016/j.imlet.2004.06.015