| pubmed-article:2038058 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2038058 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2038058 | lifeskim:mentions | umls-concept:C0019733 | lld:lifeskim |
| pubmed-article:2038058 | lifeskim:mentions | umls-concept:C0019628 | lld:lifeskim |
| pubmed-article:2038058 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2038058 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:2038058 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2038058 | pubmed:dateCreated | 1991-7-2 | lld:pubmed |
| pubmed-article:2038058 | pubmed:abstractText | The three-dimensional structure of the human histocompatibility antigen HLA-A2 was determined at 3.5 A resolution by a combination of isomorphous replacement and iterative real-space averaging of two crystal forms. The monoclinic crystal form has now been refined by least-squares methods to an R-factor of 0.169 for data from 6 to 2.6 A resolution. A superposition of the structurally similar domains found in the heterodimer, alpha 1 onto alpha 2 and alpha 3 onto beta 2m, as well as the latter pair onto the ancestrally related immunoglobulin constant domain, reveals that differences are mainly in the turn regions. Structural features of the alpha 1 and alpha 2 domains, such as conserved salt-bridges that contribute to stability, specific loops that form contacts with other domains, and the antigen-binding groove formed from two adjacent helical regions on top of an eight-stranded beta-sheet, are analyzed. The interfaces between the domains, especially those between beta 2m and the HLA heavy chain presumably involved in beta 2m exchange and heterodimer assembly, are described in detail. A detailed examination of the binding groove confirms that the solvent-accessible amino acid side-chains that are most polymorphic in mouse and human alleles fill up the central and widest portion of the binding groove, while conserved side-chains are clustered at the narrower ends of the groove. Six pockets or sub-sites in the antigen-binding groove, of diverse shape and composition, appear suited for binding side-chains from antigenic peptides. Three pockets contain predominantly non-polar atoms; but others, especially those at the extreme ends of the groove, have clusters of polar atoms in close proximity to the "extra" electron density in the binding site. A possible role for beta 2m in stabilizing permissible peptide complexes during folding and assembly is presented. | lld:pubmed |
| pubmed-article:2038058 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2038058 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2038058 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2038058 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2038058 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2038058 | pubmed:month | May | lld:pubmed |
| pubmed-article:2038058 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:2038058 | pubmed:author | pubmed-author:SaperM AMA | lld:pubmed |
| pubmed-article:2038058 | pubmed:author | pubmed-author:BjorkmanP JPJ | lld:pubmed |
| pubmed-article:2038058 | pubmed:author | pubmed-author:WileyD CDC | lld:pubmed |
| pubmed-article:2038058 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2038058 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:2038058 | pubmed:volume | 219 | lld:pubmed |
| pubmed-article:2038058 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2038058 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2038058 | pubmed:pagination | 277-319 | lld:pubmed |
| pubmed-article:2038058 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2038058 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2038058 | pubmed:articleTitle | Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. | lld:pubmed |
| pubmed-article:2038058 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138. | lld:pubmed |
| pubmed-article:2038058 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2038058 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2038058 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2038058 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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