X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.

Article Details

Citation

Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM

X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.

Science. 1998 May 22;280(5367):1277-81.

PubMed ID
9596584 [ View in PubMed
]
Abstract

Activation and covalent attachment of complement component C3 to pathogens is the key step in complement-mediated host defense. Additionally, the antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also known as CD21) on B cells and thereby contributes to the initiation of an acquired humoral response. The x-ray crystal structure of human C3d solved at 2.0 angstroms resolution reveals an alpha-alpha barrel with the residues responsible for thioester formation and covalent attachment at one end and an acidic pocket at the other. The structure supports a model whereby the transition of native C3 to its functionally active state involves the disruption of a complementary domain interface and provides insight into the basis for the interaction between C3d and CR2.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Complement C3P01024Details