2gys: Difference between revisions
New page: left|200px<br /> <applet load="2gys" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gys, resolution 2.70Å" /> '''2.7 A structure of ... |
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[[Image:2gys.gif|left|200px]]<br /> | [[Image:2gys.gif|left|200px]]<br /><applet load="2gys" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2gys, resolution 2.70Å" /> | caption="2gys, resolution 2.70Å" /> | ||
'''2.7 A structure of the extracellular domains of the human beta common receptor involved in IL-3, IL-5, and GM-CSF signalling'''<br /> | '''2.7 A structure of the extracellular domains of the human beta common receptor involved in IL-3, IL-5, and GM-CSF signalling'''<br /> | ||
==Overview== | ==Overview== | ||
X-ray diffraction has been used to produce and refine a model of the | X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule. | ||
==About this Structure== | ==About this Structure== | ||
2GYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2GYS is a [http://en.wikipedia.org/wiki/Single_protein 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=2GYS OCA]. | ||
==Reference== | ==Reference== | ||
An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope., Carr PD, Conlan F, Ford S, Ollis DL, Young IG, Acta | An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope., Carr PD, Conlan F, Ford S, Ollis DL, Young IG, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):509-13. Epub 2006 May 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16754968 16754968] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Carr, P | [[Category: Carr, P D.]] | ||
[[Category: Conlan, F.]] | [[Category: Conlan, F.]] | ||
[[Category: Ford, S.]] | [[Category: Ford, S.]] | ||
[[Category: Ollis, D | [[Category: Ollis, D L.]] | ||
[[Category: Young, I | [[Category: Young, I G.]] | ||
[[Category: dimer of interlocking chains of fibronectin-iii domains]] | [[Category: dimer of interlocking chains of fibronectin-iii domains]] | ||
[[Category: four fibronectin-iii domains per chain]] | [[Category: four fibronectin-iii domains per chain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:35 2008'' | ||
Revision as of 15:36, 21 February 2008
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2.7 A structure of the extracellular domains of the human beta common receptor involved in IL-3, IL-5, and GM-CSF signalling
Overview
X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.
About this Structure
2GYS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope., Carr PD, Conlan F, Ford S, Ollis DL, Young IG, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):509-13. Epub 2006 May 31. PMID:16754968
Page seeded by OCA on Thu Feb 21 17:36:35 2008
