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PMID: 11050405 Published · ppublish English Journal Article Review

Cooperativity: action at a distance in a classic system.

Current biology : CB ·Vol. 10 ·No. 19 ·2000-10-05 ·Pages R704-7

Koudelka GB

Abstract

A new high resolution crystal structure of the phage lambda repressor reveals the basis for repressor dimer formation and, together with biochemical data, provides insights into the mechanism of repressor tetramer formation, a process essential to the cooperative binding and gene regulatory activities of this protein.

MeSH Terms
DNA/metabolism DNA-Binding Proteins Dimerization Hydrolysis Models, Molecular Protein Binding Rec A Recombinases/metabolism Repressor Proteins/chemistry,metabolism Viral Proteins Viral Regulatory and Accessory Proteins
Chemicals
DNA-Binding Proteins Repressor Proteins Viral Proteins Viral Regulatory and Accessory Proteins phage repressor proteins DNA Rec A Recombinases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Koudelka G B
Department of Biological Sciences, State University of New York at Buffalo, Cooke Hall, North Campus, Buffalo, New York 14260-1300, USA. koudelka@acsu.buffalo.edu
Article Info
Journal
Current biology : CB
Abbr.
Curr Biol
ISSN
0960-9822
DOI
10.1016/s0960-9822(00)00710-7
Email
koudelka@acsu.buffalo.edu
Published
2000-10-05
Pages
R704-7
Language
English
Region
England
NLM ID
9107782
Subset
IM
External Links
PubMed source DOI: 10.1016/s0960-9822(00)00710-7 View journal details
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