Cited by 506Protein Structure and DynamicsGenomics and Chromatin DynamicsEnzyme Structure and Function

Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules

Klemm, Juli D., Rould, Mark A., Aurora, Rajeev, Herr, Winship, Pabo, Carl O.·1994·Cell

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.

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Crossref · 10.1016/0092-8674(94)90231-3

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58 of 58 references verified0 citation errors · 0 not checkable

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Authors
Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., & Pabo, C. O.
Affiliations
  • Massachusetts Institute of Technology (US)
  • Howard Hughes Medical Institute (US)
  • Cold Spring Harbor Laboratory (US)
Venue
Cell
Publisher
Elsevier BV
Published
1994-04
Volume
77
Issue
1
Pages
21-32
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2004689349
Cited by
506
References
58
Citations by year
2026: 3 · 2025: 8 · 2024: 7 · 2023: 1 · 2022: 3 · 2021: 5 · 2020: 7 · 2019: 3 · 2018: 7 · 2017: 9 · 2016: 9 · 2015: 5 · 2014: 8 · 2013: 11 · 2012: 7
FWCI
19.49
Type
journal article
Language
en
Open access
closed
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
  • Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
Funders
  • National Institutes of Health (5r01gm031471-16)
  • U.S. Public Health Service (5-T32-6MO7287-18)
  • National Cancer Institute (CA13106, P01CA013106)
  • National Institute of General Medical Sciences (GM-31471)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
Oct-1, POU domain, protein-DNA recognition, homeodomain, cooperative DNA binding, transcription factor-DNA complex
MeSH terms
Amino Acid Sequence, Base Sequence, Binding Sites, Deoxyribonucleoproteins, DNA, DNA-Binding Proteins, Molecular Sequence Data, Nucleic Acid Conformation, Repressor Proteins, Transcription Factors, Protein Structure, Tertiary, Crystallography, X-Ray, Octamer Transcription Factor-1, Host Cell Factor C1

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