1C3D

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

Summary for 1C3D

• Entry DOI: 10.2210/pdb1c3d/pdb
• Descriptor: C3D, GLYCEROL (3 entities in total)
• Functional Keywords: complement, c3, c3d, alpha-alpha barrel
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P01024
• Total number of polymer chains: 1
• Total formula weight: 33359.20

Authors

Nagar, B.,Jones, R.G.,Diefenbach, R.J.,Isenman, D.E.,Rini, J.M. (deposition date: 1998-05-19, release date: 1998-10-07, Last modification date: 2024-10-16)

Primary citation

Nagar, B.,Jones, R.G.,Diefenbach, R.J.,Isenman, D.E.,Rini, J.M.
X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.
Science, 280:1277-1281, 1998

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.

PubMed: 9596584
DOI: 10.1126/science.280.5367.1277

Experimental method

X-RAY DIFFRACTION (1.8 Å)