1oct
From Proteopedia
(New page: 200px<br /> <applet load="1oct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oct, resolution 3.000Å" /> '''CRYSTAL STRUCTURE ...) |
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| - | [[Image:1oct.gif|left|200px]]<br /> | + | [[Image:1oct.gif|left|200px]]<br /><applet load="1oct" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oct" size=" | + | |
caption="1oct, resolution 3.000Å" /> | caption="1oct, resolution 3.000Å" /> | ||
'''CRYSTAL STRUCTURE OF THE OCT-1 POU DOMAIN BOUND TO AN OCTAMER SITE: DNA RECOGNITION WITH TETHERED DNA-BINDING MODULES'''<br /> | '''CRYSTAL STRUCTURE OF THE OCT-1 POU DOMAIN BOUND TO AN OCTAMER SITE: DNA RECOGNITION WITH TETHERED DNA-BINDING MODULES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of an Oct-1 POU domain-octamer DNA complex has been solved | + | The structure of an Oct-1 POU domain-octamer DNA complex has been solved at 3.0 A resolution. The POU-specific domain contacts the 5' half of this site (ATGCAAAT), and as predicted from nuclear magnetic resonance studies, the structure, docking, and contacts are remarkably similar to those of the lambda and 434 repressors. The POU homeodomain contacts the 3' half of this site (ATGCAAAT), and the docking is similar to that of the engrailed, MAT alpha 2, and Antennapedia homeodomains. The linker region is not visible and there are no protein-protein contacts between the domains, but overlapping phosphate contacts near the center of the octamer site may favor cooperative binding. This novel arrangement raises important questions about cooperativity in protein-DNA recognition. |
==About this Structure== | ==About this Structure== | ||
| - | 1OCT 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:// | + | 1OCT 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=1OCT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aurora, R.]] | [[Category: Aurora, R.]] | ||
[[Category: Herr, W.]] | [[Category: Herr, W.]] | ||
| - | [[Category: Klemm, J | + | [[Category: Klemm, J D.]] |
| - | [[Category: Pabo, C | + | [[Category: Pabo, C O.]] |
| - | [[Category: Rould, M | + | [[Category: Rould, M A.]] |
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:10 2008'' |
Revision as of 12:16, 21 February 2008
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CRYSTAL STRUCTURE OF THE OCT-1 POU DOMAIN BOUND TO AN OCTAMER SITE: DNA RECOGNITION WITH TETHERED DNA-BINDING MODULES
Overview
The structure of an Oct-1 POU domain-octamer DNA complex has been solved at 3.0 A resolution. The POU-specific domain contacts the 5' half of this site (ATGCAAAT), and as predicted from nuclear magnetic resonance studies, the structure, docking, and contacts are remarkably similar to those of the lambda and 434 repressors. The POU homeodomain contacts the 3' half of this site (ATGCAAAT), and the docking is similar to that of the engrailed, MAT alpha 2, and Antennapedia homeodomains. The linker region is not visible and there are no protein-protein contacts between the domains, but overlapping phosphate contacts near the center of the octamer site may favor cooperative binding. This novel arrangement raises important questions about cooperativity in protein-DNA recognition.
About this Structure
1OCT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules., Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO, Cell. 1994 Apr 8;77(1):21-32. PMID:8156594
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