Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules.
Details
Serval ID
serval:BIB_B287EBA978C6
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules.
Journal
Cell
ISSN
0092-8674
Publication state
Published
Issued date
04/1994
Peer-reviewed
Oui
Volume
77
Number
1
Pages
21-32
Language
english
Abstract
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.
Keywords
Amino Acid Sequence, Base Sequence, Binding Sites, Crystallography, X-Ray, DNA, DNA-Binding Proteins, Deoxyribonucleoproteins, Host Cell Factor C1, Molecular Sequence Data, Nucleic Acid Conformation, Octamer Transcription Factor-1, Protein Structure, Tertiary, Repressor Proteins, Transcription Factors
Pubmed
Web of science
Create date
24/01/2008 16:36
Last modification date
20/08/2019 16:21
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