1bf5
From Proteopedia
(New page: 200px<br /> <applet load="1bf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bf5, resolution 2.900Å" /> '''TYROSINE PHOSPHORY...) |
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| - | [[Image:1bf5.gif|left|200px]]<br /> | + | [[Image:1bf5.gif|left|200px]]<br /><applet load="1bf5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bf5" size=" | + | |
caption="1bf5, resolution 2.900Å" /> | caption="1bf5, resolution 2.900Å" /> | ||
'''TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX'''<br /> | '''TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the DNA complex of a STAT-1 homodimer has been | + | The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BF5 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:// | + | 1BF5 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=1BF5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, X.]] | [[Category: Chen, X.]] | ||
[[Category: Jeruzalmi, D.]] | [[Category: Jeruzalmi, D.]] | ||
| - | [[Category: Jr., J | + | [[Category: Jr., J E.Darnell.]] |
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: Vinkemeier, U.]] | [[Category: Vinkemeier, U.]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:36 2008'' |
Revision as of 09:54, 21 February 2008
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TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX
Contents |
Overview
The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.
Disease
Known diseases associated with this structure: Mycobacterial infection, atypical, familial disseminated OMIM:[600555], STAT1 deficiency, complete OMIM:[600555]
About this Structure
1BF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA., Chen X, Vinkemeier U, Zhao Y, Jeruzalmi D, Darnell JE Jr, Kuriyan J, Cell. 1998 May 29;93(5):827-39. PMID:9630226
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