title: Cooperativity: action at a distance in a classic system.
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.
authors.affiliation: 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
authors.forename: G B
authors.initials: GB
authors.lastname: Koudelka
mesh_terms: D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins; D019281:Dimerization; D006868:Hydrolysis; D008958:Models, Molecular; D011485:Protein Binding; D011938:Rec A Recombinases / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
chemical_list: D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins; D004247:DNA; D011938:Rec A Recombinases