1hf0: Difference between revisions

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[[Image:1hf0.~~gif~~|left|200px]]

[[Image:1hf0.png|left|200px]]

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~~'''~~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

(as it appears on PubMed at http://www.pubmed.gov), where 11583619 is the PubMed ID number.

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==About this Structure==

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[[Category: Oct-1]]

[[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''

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-[[Image:1hf0.gif|left|200px]]
+{{Seed}}
+[[Image:1hf0.png|left|200px]]
 <!--
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 {{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==
+<!--
-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
+(as it appears on PubMed at http://www.pubmed.gov), where 11583619 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11583619}}
 ==About this Structure==
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 [[Category: Oct-1]]
 [[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''