Cooperativity: Action at a distance in a classic system

A new high resolution crystal structure of the phage λ 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...

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Bibliographic Details
Published inCurrent biology Vol. 10; no. 19; pp. R704 - R707
Main Author Koudelka, Gerald B
Format Journal Article
LanguageEnglish
Published England Elsevier Inc 05.10.2000
Subjects
Dimerization
DNA - metabolism
DNA-Binding Proteins
Hydrolysis
Models, Molecular
Phage ^l
Protein Binding
Rec A Recombinases - metabolism
Repressor Proteins - chemistry
Repressor Proteins - metabolism
Viral Proteins
Viral Regulatory and Accessory Proteins
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Summary:A new high resolution crystal structure of the phage λ 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.
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ISSN:0960-9822
1879-0445
DOI:10.1016/S0960-9822(00)00710-7