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 furthe...

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Bibliographic Details
Published in:The EMBO journal 1991-05, Vol.10 (5), p.1053-1059
Main Authors: Rippmann, F., Taylor, W. R., Rothbard, J. B., Green, N. M.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Amino Acid Sequence
binding
Binding Sites
Biological and medical sciences
Chymotrypsin
domains
Fundamental and applied biological sciences. Psychology
Genic rearrangement. Recombination. Transposable element
Heat-Shock Proteins - chemistry
histocompatibility antigen-HLA
HLA-A2 Antigen - chemistry
Hsp70 protein
Humans
Hydrolysis
Models, Molecular
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Protein Conformation
Sequence Homology, Nucleic Acid
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Summary: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.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1991.tb08044.x