Crystal-Structure of the Oct-1 Pou Domain Bound to an Octamer Site - DNA Recognition with Tethered DNA-Binding Modules

Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., Pabo, C. O. (1994) Crystal-Structure of the Oct-1 Pou Domain Bound to an Octamer Site - DNA Recognition with Tethered DNA-Binding Modules. Cell, 77 (1). pp. 21-32. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/8156594
DOI: 10.1016/0092-8674(94)90231-3

Abstract

The structure of an Oct-1 POU domain-octamer DNA complex has been solved at 3.0 Angstrom resolution. The POU-specific domain contacts the 5' half of this site (ATG- CAAAT), 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.

Item Type: Paper
Uncontrolled Keywords: HEAVY-CHAIN PROMOTER TRANSCRIPTION FACTOR OPERATOR COMPLEX NUCLEIC-ACIDS AMINO-ACID I-POU HOMEODOMAIN PROTEIN SPECIFICITY RESOLUTION
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date Deposited: 19 May 2015 20:41
Last Modified: 19 May 2015 20:41
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31461

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