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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| Veröffentlicht in: | The EMBO journal 1991-05, Vol.10 (5), p.1053-1059 |
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| container_title | The EMBO journal |
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| creator | Rippmann, F. Taylor, W. R. Rothbard, J. B. Green, N. M. |
| description | 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. |
| doi_str_mv | 10.1002/j.1460-2075.1991.tb08044.x |
| format | Article |
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R.</creatorcontrib><creatorcontrib>Rothbard, J. B.</creatorcontrib><creatorcontrib>Green, N. M.</creatorcontrib><title>A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>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.</description><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>binding</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Chymotrypsin</subject><subject>domains</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genic rearrangement. Recombination. Transposable element</subject><subject>Heat-Shock Proteins - chemistry</subject><subject>histocompatibility antigen-HLA</subject><subject>HLA-A2 Antigen - chemistry</subject><subject>Hsp70 protein</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Models, Molecular</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkVFv0zAUhS0EGmXwE5AsJHhLdu3Yjo3EQ5nGNtSJF3i2HNtpXSVxiFNY_z0pjcp4mvbkK59zro_1IfSOQE4A6MU2J0xARqHkOVGK5GMFEhjL75-hxUl6jhZABckYkeolepXSFgC4LMkZOqNAKZF0gdZLvNn3cdz4MVjT4DY63-A6Dni6wr3vx-A8rkLnQrfGLrYmdDjWeJP6EnBlknc4do-Yb1bL1-hFbZrk38znOfrx5er75U22-nZ9e7lcZVYAZ1lZ0LIiXDErOeOSMWVqQa2tBC0crTgHBlRRaqByTBrmvRNUAihCRC0KUpyjT8e9_a5qvbO-GwfT6H4IrRn2Opqg_1e6sNHr-EszTkteTvkPc36IP3c-jboNyfqmMZ2Pu6Ql8IJLwR81EiGYFKWajB-PRjvElAZfn8oQ0AeceqsPzPSBmT7g1DNOfT-F3z78zik685v097Nu0oSvHkxnQ_r3guLlXGJ59P0Ojd8_oYG-uvv89e9c_AE_P7yO</recordid><startdate>199105</startdate><enddate>199105</enddate><creator>Rippmann, F.</creator><creator>Taylor, W. 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M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6054-7327b1594c85458449af62ccb623d2b550402922a0bd48a4eed628009116f6313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Adenosine Triphosphate - chemistry</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>binding</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Chymotrypsin</topic><topic>domains</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genic rearrangement. Recombination. 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M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1991-05</date><risdate>1991</risdate><volume>10</volume><issue>5</issue><spage>1053</spage><epage>1059</epage><pages>1053-1059</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><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.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>2022182</pmid><doi>10.1002/j.1460-2075.1991.tb08044.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| 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 |
| title | A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA |
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