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

Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM
Science 280 1277-81 (1998)
Cited: 136 times
EuropePMC logo PMID: 9596584

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.

Reviews - 1c3d mentioned but not cited (6)

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Articles - 1c3d mentioned but not cited (31)

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Reviews citing this publication (21)

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