title: Allostery in the Hsp70 chaperone proteins.
abstract: Heat shock 70-kDa (Hsp70) chaperones are essential to in vivo protein folding, protein transport, and protein re-folding. They carry out these activities using repeated cycles of binding and release of client proteins. This process is under allosteric control of nucleotide binding and hydrolysis. X-ray crystallography, NMR spectroscopy, and other biophysical techniques have contributed much to the understanding of the allosteric mechanism linking these activities and the effect of co-chaperones on this mechanism. In this chapter these findings are critically reviewed. Studies on the allosteric mechanisms of Hsp70 have gained enhanced urgency, as recent studies have implicated this chaperone as a potential drug target in diseases such as Alzheimer's and cancer. Recent approaches to combat these diseases through interference with the Hsp70 allosteric mechanism are discussed.
authors.affiliation: Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, USA. zuiderwe@umich.edu
authors.forename: Erik R P
authors.initials: ER
authors.lastname: Zuiderweg
authors.forename: Eric B
authors.initials: EB
authors.lastname: Bertelsen
authors.forename: Aikaterini
authors.initials: A
authors.lastname: Rousaki
authors.forename: Matthias P
authors.initials: MP
authors.lastname: Mayer
authors.forename: Jason E
authors.initials: JE
authors.lastname: Gestwicki
authors.forename: Atta
authors.initials: A
authors.lastname: Ahmad
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D018360:Crystallography, X-Ray; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008958:Models, Molecular
chemical_list: D018840:HSP70 Heat-Shock Proteins; D000255:Adenosine Triphosphate