2vsd: Difference between revisions
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==crystal structure of CHIR-AB1== | ==crystal structure of CHIR-AB1== | ||
<StructureSection load='2vsd' size='340' side='right' caption='[[2vsd]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='2vsd' size='340' side='right'caption='[[2vsd]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vsd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VSD FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vsd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VSD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsd OCA], [http://pdbe.org/2vsd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vsd RCSB], [http://www.ebi.ac.uk/pdbsum/2vsd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsd ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsd OCA], [http://pdbe.org/2vsd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vsd RCSB], [http://www.ebi.ac.uk/pdbsum/2vsd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Chick]] | [[Category: Chick]] | ||
[[Category: Large Structures]] | |||
[[Category: Arnon, T I]] | [[Category: Arnon, T I]] | ||
[[Category: Bjorkman, P J]] | [[Category: Bjorkman, P J]] | ||
Revision as of 10:13, 23 October 2019
crystal structure of CHIR-AB1crystal structure of CHIR-AB1
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCHIR-AB1 is a newly identified avian immunoglobulin (Ig) receptor that includes both activating and inhibitory motifs and was therefore classified as a potentially bifunctional receptor. Recently, CHIR-AB1 was shown to bind the Fc region of chicken IgY and to induce calcium mobilization via association with the common gamma-chain, a subunit that transmits signals upon ligation of many different immunoreceptors. Here we describe the 1.8-A-resolution crystal structure of the CHIR-AB1 ectodomain. The receptor ectodomain consists of a single C2-type Ig domain resembling the Ig-like domains found in mammalian Fc receptors such as FcgammaRs and FcalphaRI. Unlike these receptors and other monomeric Ig superfamily members, CHIR-AB1 crystallized as a 2-fold symmetrical homodimer that bears no resemblance to variable or constant region dimers in an antibody. Analytical ultracentrifugation demonstrated that CHIR-AB1 exists as a mixture of monomers and dimers in solution, and equilibrium gel filtration revealed a 2:1 receptor/ligand binding stoichiometry. Measurement of the 1:1 CHIR-AB1/IgY interaction affinity indicates a relatively low affinity complex, but a 2:1 CHIR-AB1/IgY interaction allows an increase in apparent affinity due to avidity effects when the receptor is tethered to a surface. Taken together, these results add to the structural understanding of Fc receptors and their functional mechanisms. The crystal structure of CHIR-AB1: a primordial avian classical Fc receptor.,Arnon TI, Kaiser JT, West AP Jr, Olson R, Diskin R, Viertlboeck BC, Gobel TW, Bjorkman PJ J Mol Biol. 2008 Sep 12;381(4):1012-24. Epub 2008 Jul 3. PMID:18625238[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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