1c3d: Difference between revisions
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[[Image:1c3d.gif|left|200px]] | [[Image:1c3d.gif|left|200px]] | ||
'''X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2''' | {{Structure | ||
|PDB= 1c3d |SIZE=350|CAPTION= <scene name='initialview01'>1c3d</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C3D is a [ | 1C3D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3D OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9596584 9596584] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: complement]] | [[Category: complement]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:16 2008'' | ||
Revision as of 08:19, 20 March 2008
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| 1c3d, resolution 1.80Å | |||||||||||||
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| Ligands: | GOL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2
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. 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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