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1fnl

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(New page: 200px<br /> <applet load="1fnl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnl, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fnl.gif|left|200px]]<br />
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[[Image:1fnl.gif|left|200px]]<br /><applet load="1fnl" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1fnl" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1fnl, resolution 1.8&Aring;" />
caption="1fnl, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII'''<br />
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1FNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNL OCA].
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1FNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNL OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Boesen, C.C.]]
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[[Category: Boesen, C C.]]
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[[Category: Brooks, A.G.]]
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[[Category: Brooks, A G.]]
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[[Category: Fridman, W.H.]]
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[[Category: Fridman, W H.]]
[[Category: Radaev, S.]]
[[Category: Radaev, S.]]
[[Category: Sautes-Fridman, C.]]
[[Category: Sautes-Fridman, C.]]
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[[Category: Sun, P.D.]]
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[[Category: Sun, P D.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
[[Category: HG]]
[[Category: HG]]
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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:55:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:38 2008''

Revision as of 10:40, 21 February 2008


1fnl, resolution 1.8Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII

Contents

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 with as ligand. 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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