Different peptide binding specificities of hsp70 family members.
A set of heptapeptides was used to compare the relative peptide affinities of three proteins of the hsp70 family: bacterial DnaK, mammalian cytosolic hsc70, and BiP from mammalian ER. Each hsp displays a characteristic pattern of relative affinities. DnaK and hsc70 are more similar to each other than to BiP. A difference in peptide binding specificity may be an important determinant in adjusting an hsp70 family member to its particular cellular function.
Gragerov
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Institute of Cancer Research, College of Physicians and Surgeons, Columbia University, New York, NY 10032.
Gottesman
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ME
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D006224:Cricetinae; D029968:Escherichia coli Proteins; D005656:Fungal Proteins / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C060153:KAR2 protein, yeast; D009842:Oligopeptides; D011994:Recombinant Proteins; C063842:dnaK protein, E coli