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'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII''' | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII''' | ||
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[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
[[Category: | [[Category: Beta sandwich]] | ||
[[Category: | [[Category: Immunoglobulin-like]] | ||
[[Category: | [[Category: Receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:32:26 2008'' | |||
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Revision as of 13:32, 2 May 2008
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.
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 Page seeded by OCA on Fri May 2 16:32:26 2008
