1c3d

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spinqualitylabelsall models 1c3d, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: C3 deficiency OMIM:[120700], Macular degeneration, age-related, 9 OMIM:[120700]

About this Structure

1C3D is a Single protein structure of sequence from Homo sapiens with GOL as ligand. Full crystallographic information is available from OCA.

Reference

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. 1998 May 22;280(5367):1277-81. PMID:9596584

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