1hf0

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(New page: 200px<br /> <applet load="1hf0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hf0, resolution 2.7&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hf0.gif|left|200px]]<br /><applet load="1hf0" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1hf0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hf0, resolution 2.7&Aring;" />
caption="1hf0, resolution 2.7&Aring;" />
'''CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER'''<br />
'''CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1HF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HF0 OCA].
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1HF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF0 OCA].
==Reference==
==Reference==
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[[Category: Pohl, E.]]
[[Category: Pohl, E.]]
[[Category: Remenyi, A.]]
[[Category: Remenyi, A.]]
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[[Category: Scholer, H.R.]]
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[[Category: Scholer, H R.]]
[[Category: Tomilin, A.]]
[[Category: Tomilin, A.]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns, M.]]
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[[Category: pou domain]]
[[Category: pou domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:17:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:37 2008''

Revision as of 11:00, 21 February 2008


1hf0, resolution 2.7Å

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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.

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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