1bg1: Difference between revisions

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New page: left|200px<br /><applet load="1bg1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bg1, resolution 2.25Å" /> '''TRANSCRIPTION FACTOR...
 
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[[Image:1bg1.gif|left|200px]]<br /><applet load="1bg1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bg1.gif|left|200px]]<br /><applet load="1bg1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bg1, resolution 2.25&Aring;" />
caption="1bg1, resolution 2.25&Aring;" />
'''TRANSCRIPTION FACTOR STAT3B/DNA COMPLEX'''<br />
'''TRANSCRIPTION FACTOR STAT3B/DNA COMPLEX'''<br />


==Overview==
==Overview==
STAT proteins are a family of eukaryotic transcription factors that, mediate the response to a large number of cytokines and growth factors., Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific, promoter sequences on their target genes. Here we report the first crystal, structure of a STAT protein bound to its DNA recognition site at 2.25 A, resolution. The structure provides insight into the various steps by which, STAT proteins deliver a response signal directly from the cell membrane to, their target genes in the nucleus.
STAT proteins are a family of eukaryotic transcription factors that mediate the response to a large number of cytokines and growth factors. Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific promoter sequences on their target genes. Here we report the first crystal structure of a STAT protein bound to its DNA recognition site at 2.25 A resolution. The structure provides insight into the various steps by which STAT proteins deliver a response signal directly from the cell membrane to their target genes in the nucleus.


==About this Structure==
==About this Structure==
1BG1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BG1 OCA].  
1BG1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG1 OCA].  


==Reference==
==Reference==
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[[Category: Becker, S.]]
[[Category: Becker, S.]]
[[Category: Groner, B.]]
[[Category: Groner, B.]]
[[Category: Muller, C.W.]]
[[Category: Muller, C W.]]
[[Category: complex (transcription factor/dna)]]
[[Category: complex (transcription factor/dna)]]
[[Category: cytokine activation]]
[[Category: cytokine activation]]
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[[Category: transcription factor]]
[[Category: transcription factor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:37:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:52 2008''

Revision as of 12:54, 21 February 2008

File:1bg1.gif


1bg1, resolution 2.25Å

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TRANSCRIPTION FACTOR STAT3B/DNA COMPLEX

OverviewOverview

STAT proteins are a family of eukaryotic transcription factors that mediate the response to a large number of cytokines and growth factors. Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific promoter sequences on their target genes. Here we report the first crystal structure of a STAT protein bound to its DNA recognition site at 2.25 A resolution. The structure provides insight into the various steps by which STAT proteins deliver a response signal directly from the cell membrane to their target genes in the nucleus.

About this StructureAbout this Structure

1BG1 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the Stat3beta homodimer bound to DNA., Becker S, Groner B, Muller CW, Nature. 1998 Jul 9;394(6689):145-51. PMID:9671298

Page seeded by OCA on Thu Feb 21 11:54:52 2008

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