1hf0: Difference between revisions

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[[Image:1hf0.gif|left|200px]]
{{Seed}}
[[Image:1hf0.png|left|200px]]


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{{STRUCTURE_1hf0|  PDB=1hf0  |  SCENE=  }}  
{{STRUCTURE_1hf0|  PDB=1hf0  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER'''
===CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER===




==Overview==
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Two crystal structures of Oct-1 POU domain bound to DNA provide a rationale for differential, conformation-dependent recruitment of transcription cofactors. The POU-homeo and POU-specific subdomains of Oct-1 contain two different nonoverlapping pairs of surface patches that are capable of forming unrelated protein-protein interfaces. Members of the POU factor family contain one or two conserved sequence motifs in the interface that are known to be phosphorylated, as noted for Oct-1 and Pit-1. Modeling of Oct-4 reveals the unique case where the same conserved sequence is located in both interfaces. Our studies provide the basis for two distinct dimeric POU factor arrangements that are dictated by the architecture of each DNA response element. We suggest interface swapping in dimers could be a general mechanism of modulating the activity of transcription factors.
The line below this paragraph, {{ABSTRACT_PUBMED_11583619}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11583619}}


==About this Structure==
==About this Structure==
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[[Category: Oct-1]]
[[Category: Oct-1]]
[[Category: Pou domain]]
[[Category: Pou domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:47:00 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:05:56 2008''

Revision as of 05:05, 1 July 2008

File:1hf0.png

Template:STRUCTURE 1hf0

CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER

Template:ABSTRACT PUBMED 11583619

About this Structure

1HF0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping., Remenyi A, Tomilin A, Pohl E, Lins K, Philippsen A, Reinbold R, Scholer HR, Wilmanns M, Mol Cell. 2001 Sep;8(3):569-80. PMID:11583619

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