1bf5

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{{STRUCTURE_1bf5| PDB=1bf5 | SCENE= }}
{{STRUCTURE_1bf5| PDB=1bf5 | SCENE= }}
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'''TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX'''
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===TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 9630226 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9630226}}
==About this Structure==
==About this Structure==
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[[Category: Sh2 domain]]
[[Category: Sh2 domain]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:26:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:01:09 2008''

Revision as of 16:01, 30 June 2008

Image:1bf5.png

Template:STRUCTURE 1bf5

TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX

Template:ABSTRACT PUBMED 9630226

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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