1fnl: Difference between revisions
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[[Image:1fnl.gif|left|200px]] | [[Image:1fnl.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII''' | {{Structure | ||
|PDB= 1fnl |SIZE=350|CAPTION= <scene name='initialview01'>1fnl</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FNL is a [ | 1FNL 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=1FNL OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the extracellular domain of a human Fc gamma RIII., Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD, Immunity. 2000 Sep;13(3):387-95. PMID:[http:// | Crystal structure of the extracellular domain of a human Fc gamma RIII., Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD, Immunity. 2000 Sep;13(3):387-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11021536 11021536] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
''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 11:11:30 2008'' | ||
Revision as of 09:11, 20 March 2008
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| 1fnl, resolution 1.8Å | |||||||||||||
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| Ligands: | HG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII
Overview
Fc receptors play a major role in immune defenses against pathogens and in inflammatory processes. The crystal structure of a human immunoglobulin receptor, FcgammaRIIIb, has been determined to 1.8 A resolution. The overall fold consists of two immunoglobulin-like domains with an acute interdomain hinge angle of approximately 50 degrees. Trp-113, wedged between the N-terminal D1 and the C-terminal D2 domains, appears to further restrict the hinge angle. The putative Fc binding region of the receptor carries a net positive charge complementary to the negative-charged receptor binding regions on Fc. A 1:1 binding stoichiometry between the receptor and Fc was measured by both the equilibrium and nonequilibrium size-exclusion chromatography. Two separate parallel dimers are observed in the crystal lattice, offering intriguing models for receptor aggregation.
Disease
Known diseases associated with this structure: Lupus erythematosus, systemic, susceptibility OMIM:[146740], Neutropenia, alloimmune neonatal OMIM:[146740], Viral infections, recurrent OMIM:[146740]
About this Structure
1FNL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the extracellular domain of a human Fc gamma RIII., Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD, Immunity. 2000 Sep;13(3):387-95. PMID:11021536
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