1oct
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(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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Revision as of 16:25, 12 November 2007
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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
Page seeded by OCA on Mon Nov 12 18:31:31 2007
