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 2.900Å" /> '''TYROSINE PHOSPHORY...)
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Revision as of 14:02, 12 November 2007
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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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