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1bf5

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(New page: 200px<br /> <applet load="1bf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bf5, resolution 2.900&Aring;" /> '''TYROSINE PHOSPHORY...)
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'''TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX'''<br />
'''TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BF5 OCA].
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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.]]
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[[Category: Jr., J.E.Darnell.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:09:03 2007''
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''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


1bf5, resolution 2.900Å

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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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