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- | [[Image:1m6o.jpg|left|200px]] | + | {{Seed}} |
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| {{STRUCTURE_1m6o| PDB=1m6o | SCENE= }} | | {{STRUCTURE_1m6o| PDB=1m6o | SCENE= }} |
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- | '''Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide'''
| + | ===Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide=== |
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- | ==Overview==
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- | HLA-B*4402 and B*4403 are naturally occurring MHC class I alleles that are both found at a high frequency in all human populations, and yet they only differ by one residue on the alpha2 helix (B*4402 Asp156-->B*4403 Leu156). CTLs discriminate between HLA-B*4402 and B*4403, and these allotypes stimulate strong mutual allogeneic responses reflecting their known barrier to hemopoeitic stem cell transplantation. Although HLA-B*4402 and B*4403 share >95% of their peptide repertoire, B*4403 presents more unique peptides than B*4402, consistent with the stronger T cell alloreactivity observed toward B*4403 compared with B*4402. Crystal structures of B*4402 and B*4403 show how the polymorphism at position 156 is completely buried and yet alters both the peptide and the heavy chain conformation, relaxing ligand selection by B*4403 compared with B*4402. Thus, the polymorphism between HLA-B*4402 and B*4403 modifies both peptide repertoire and T cell recognition, and is reflected in the paradoxically powerful alloreactivity that occurs across this "minimal" mismatch. The findings suggest that these closely related class I genes are maintained in diverse human populations through their differential impact on the selection of peptide ligands and the T cell repertoire.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12939341}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12939341 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_12939341}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mhc i]] | | [[Category: Mhc i]] |
| [[Category: Signal]] | | [[Category: Signal]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:42:08 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:19:56 2008'' |
Revision as of 20:19, 2 July 2008
Template:STRUCTURE 1m6o
Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide
Template:ABSTRACT PUBMED 12939341
About this Structure
1M6O is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A naturally selected dimorphism within the HLA-B44 supertype alters class I structure, peptide repertoire, and T cell recognition., Macdonald WA, Purcell AW, Mifsud NA, Ely LK, Williams DS, Chang L, Gorman JJ, Clements CS, Kjer-Nielsen L, Koelle DM, Burrows SR, Tait BD, Holdsworth R, Brooks AG, Lovrecz GO, Lu L, Rossjohn J, McCluskey J, J Exp Med. 2003 Sep 1;198(5):679-91. Epub 2003 Aug 25. PMID:12939341
Page seeded by OCA on Wed Jul 2 23:19:56 2008
Categories: Homo sapiens | Protein complex | Brooks, A G. | Clements, C S. | Ely, L K. | Gorman, J J. | Kjer-Nielsen, L. | Koelle, D M. | Lovrecz, G O. | Lu, L. | Macdonald, W A. | McCluskey, J. | Mifsud, N A. | Purcell, A W. | Rossjohn, J. | Williams, D S. | Glycoprotein | Mhc i | Signal