A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA.
The sequences of the peptide binding domains of 33 70 kd heat shock proteins (hsp70) have been aligned and a consensus secondary structure has been deduced. Individual members showed no significant deviation from the consensus, which showed a beta 4 alpha motif repeated twice, followed by two further helices and a terminus rich in Pro and Gly. The repeated motif could be aligned with the secondary structure of the functionally equivalent peptide binding domain of human leucocyte antigen (HLA) class I maintaining equivalent residues in structurally important positions in the two families and a model was built based on this alignment. The interaction of this domain with the ATP domain is considered. The overall model is shown to be consistent with the properties of products of chymotryptic cleavage.
Rippmann
F
F
National Institute for Medical Research, Mill Hill, London, UK.
Taylor
W R
WR
Rothbard
J B
JB
Green
N M
NM
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D002918:Chymotrypsin; D015789:HLA-A2 Antigen / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D015789:HLA-A2 Antigen; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D002918:Chymotrypsin