A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA.
- 1 May 1991
- journal article
- Published by Springer Nature in The EMBO Journal
- Vol. 10 (5) , 1053-1059
- https://doi.org/10.1002/j.1460-2075.1991.tb08044.x
Abstract
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.Keywords
This publication has 27 references indexed in Scilit:
- Prediction of protein secondary structure and active sites using the alignment of homologous sequencesPublished by Elsevier ,2004
- Secondary structure of the mammalian 70-kilodalton heat shock cognate protein analyzed by circular dichroism spectroscopy and secondary structure predictionBiochemistry, 1990
- Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysisCell, 1990
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990
- Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia: a candidate intermediate in the vesicle uncoating reaction.The Journal of cell biology, 1989
- Structure of the human class I histocompatibility antigen, HLA-A2Nature, 1987
- Uncoating ATPase is a member of the 70 kilodalton family of stress proteinsCell, 1986
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Prediction of the Secondary Structure of Proteins from their Amino Acid SequencePublished by Wiley ,1979
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978