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| - | [[Image:3hla.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_3hla| PDB=3hla | SCENE= }} | | {{STRUCTURE_3hla| PDB=3hla | SCENE= }} |
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| - | '''SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68'''
| + | ===SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_2038058}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2038058 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_2038058}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Wiley, D C.]] | | [[Category: Wiley, D C.]] |
| | [[Category: Histocompatibility antigen]] | | [[Category: Histocompatibility antigen]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:03:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:49:22 2008'' |
Revision as of 09:49, 3 July 2008
Template:STRUCTURE 3hla
SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68
Template:ABSTRACT PUBMED 2038058
About this Structure
3HLA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution., Saper MA, Bjorkman PJ, Wiley DC, J Mol Biol. 1991 May 20;219(2):277-319. PMID:2038058
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