Molecular chaperones. Panning for chaperone-binding peptides.
Experiments designed to define the substrate-binding preferences of the molecular chaperone BiP show that bound peptides are characterized by a heptameric motif with alternating hydrophobic residues.
Gierasch
L M
LM
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235-9041.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D018834:Chaperonin 60 / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D017433:Protein Structure, Secondary
D018834:Chaperonin 60; D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C060153:KAR2 protein, yeast; D000255:Adenosine Triphosphate