1bgf
From Proteopedia
(New page: 200px<br /><applet load="1bgf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bgf, resolution 1.45Å" /> '''STAT-4 N-DOMAIN'''<b...) |
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| - | [[Image:1bgf.gif|left|200px]]<br /><applet load="1bgf" size=" | + | [[Image:1bgf.gif|left|200px]]<br /><applet load="1bgf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bgf, resolution 1.45Å" /> | caption="1bgf, resolution 1.45Å" /> | ||
'''STAT-4 N-DOMAIN'''<br /> | '''STAT-4 N-DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | STATs (signal transducers and activators of transcription) are a family of | + | STATs (signal transducers and activators of transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. The crystal structure of an NH2-terminal conserved domain (N-domain) comprising the first 123 residues of STAT-4 was determined at 1.45 angstroms. The domain consists of eight helices that are assembled into a hook-like structure. The N-domain has been implicated in several protein-protein interactions affecting transcription, and it enables dimerized STAT molecules to polymerize and to bind DNA cooperatively. The structure shows that N-domains can interact through an extensive interface formed by polar interactions across one face of the hook. Mutagenesis of an invariant tryptophan residue at the heart of this interface abolished cooperative DNA binding by the full-length protein in vitro and reduced the transcriptional response after cytokine stimulation in vivo. |
==About this Structure== | ==About this Structure== | ||
| - | 1BGF 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:// | + | 1BGF 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=1BGF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Darnell, J | + | [[Category: Darnell, J E.]] |
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: Moarefi, I.]] | [[Category: Moarefi, I.]] | ||
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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 11:55:00 2008'' |
Revision as of 09:55, 21 February 2008
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STAT-4 N-DOMAIN
Overview
STATs (signal transducers and activators of transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. The crystal structure of an NH2-terminal conserved domain (N-domain) comprising the first 123 residues of STAT-4 was determined at 1.45 angstroms. The domain consists of eight helices that are assembled into a hook-like structure. The N-domain has been implicated in several protein-protein interactions affecting transcription, and it enables dimerized STAT molecules to polymerize and to bind DNA cooperatively. The structure shows that N-domains can interact through an extensive interface formed by polar interactions across one face of the hook. Mutagenesis of an invariant tryptophan residue at the heart of this interface abolished cooperative DNA binding by the full-length protein in vitro and reduced the transcriptional response after cytokine stimulation in vivo.
About this Structure
1BGF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the amino-terminal protein interaction domain of STAT-4., Vinkemeier U, Moarefi I, Darnell JE Jr, Kuriyan J, Science. 1998 Feb 13;279(5353):1048-52. PMID:9461439
Page seeded by OCA on Thu Feb 21 11:55:00 2008
