1yvl
From Proteopedia
(New page: 200px<br /> <applet load="1yvl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yvl, resolution 3.0Å" /> '''Structure of Unphosp...) |
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| - | [[Image:1yvl.gif|left|200px]]<br /> | + | [[Image:1yvl.gif|left|200px]]<br /><applet load="1yvl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yvl" size=" | + | |
caption="1yvl, resolution 3.0Å" /> | caption="1yvl, resolution 3.0Å" /> | ||
'''Structure of Unphosphorylated STAT1'''<br /> | '''Structure of Unphosphorylated STAT1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure has been determined at 3.0 A resolution for an | + | The crystal structure has been determined at 3.0 A resolution for an unphosphorylated STAT1 (1-683) complexed with a phosphopeptide derived from the alpha chain of interferon gamma (IFNgamma) receptor. Two dimer interfaces are seen, one between the N domains (NDs) (amino acid residues 1-123) and the other between the core fragments (CFs) (residues 132-683). Analyses of the wild-type (wt) and mutant STAT1 proteins by static light scattering, analytical ultracentrifugation, and coimmunoprecipitation suggest that STAT1 is predominantly dimeric prior to activation, and the dimer is mediated by the ND interactions. The connecting region between the ND and the CF is flexible and allows two interconvertable orientations of the CFs, termed "antiparallel" or "parallel," as determined by SH2 domain orientations. Functional implications of these dimer conformations are discussed. Also revealed in this structure is the detailed interaction between STAT1 SH2 domain and its docking site on IFNgamma receptor. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YVL 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 AU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YVL 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=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, X.]] | [[Category: Chen, X.]] | ||
[[Category: Demeler, B.]] | [[Category: Demeler, B.]] | ||
| - | [[Category: Jr., J | + | [[Category: Jr., J E.Darnell.]] |
[[Category: Mao, X.]] | [[Category: Mao, X.]] | ||
| - | [[Category: McMurray, J | + | [[Category: McMurray, J S.]] |
| - | [[Category: Parker, G | + | [[Category: Parker, G N.]] |
| - | [[Category: Pastorello, M | + | [[Category: Pastorello, M A.]] |
[[Category: Ren, Z.]] | [[Category: Ren, Z.]] | ||
[[Category: Sondermann, H.]] | [[Category: Sondermann, H.]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:34 2008'' |
Revision as of 14:09, 21 February 2008
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Structure of Unphosphorylated STAT1
Contents |
Overview
The crystal structure has been determined at 3.0 A resolution for an unphosphorylated STAT1 (1-683) complexed with a phosphopeptide derived from the alpha chain of interferon gamma (IFNgamma) receptor. Two dimer interfaces are seen, one between the N domains (NDs) (amino acid residues 1-123) and the other between the core fragments (CFs) (residues 132-683). Analyses of the wild-type (wt) and mutant STAT1 proteins by static light scattering, analytical ultracentrifugation, and coimmunoprecipitation suggest that STAT1 is predominantly dimeric prior to activation, and the dimer is mediated by the ND interactions. The connecting region between the ND and the CF is flexible and allows two interconvertable orientations of the CFs, termed "antiparallel" or "parallel," as determined by SH2 domain orientations. Functional implications of these dimer conformations are discussed. Also revealed in this structure is the detailed interaction between STAT1 SH2 domain and its docking site on IFNgamma receptor.
Disease
Known diseases associated with this structure: Mycobacterial infection, atypical, familial disseminated OMIM:[600555], STAT1 deficiency, complete OMIM:[600555]
About this Structure
1YVL is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural bases of unphosphorylated STAT1 association and receptor binding., Mao X, Ren Z, Parker GN, Sondermann H, Pastorello MA, Wang W, McMurray JS, Demeler B, Darnell JE Jr, Chen X, Mol Cell. 2005 Mar 18;17(6):761-71. PMID:15780933
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