Molecular chaperones: How J domains turn on Hsp70s.
Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.
Kelley
W L
WL
Département de Biochimie Médicale, CMU-Université de Genève, 1 rue Michel-Servet, 1211 Genève 4, Switzerland. William.Kelley@medecine.unige.ch
D001665:Binding Sites; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones