AI Article Synopsis
- C1q is a key protein in the classical complement pathway, linking innate and acquired immunity by recognizing various ligands with its gC1q domain.
- The gC1q domain has a unique jelly-roll structure similar to that of the TNF ligand family, indicating its role in the C1q and TNF superfamily.
- This review updates our understanding of the structure and function of the gC1q domain in human C1q and highlights the variety of proteins that utilize this domain for multiple functions.
Article Abstract
C1q 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, C1q can engage a broad range of self and non-self ligands via its heterotrimeric globular (gC1q) domain and thus trigger the classical pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. The X-ray crystal structures of the gC1q domain of a few members of the C1q family reveal a compact jelly-roll beta-sandwich fold similar to that of the multifunctional tumor necrosis factor (TNF) ligand family, hence the C1q and TNF superfamily. This review is an update on the structural and functional aspects of the gC1q domain of human C1q. We also mention the diverse range of proteins that utilize a gC1q domain in order to reflect on its importance as a versatile scaffold to support a variety of functions.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.imbio.2006.11.001 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!