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1m6o

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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'''
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===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--&gt;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 &gt;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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12939341 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12939341}}
==About this Structure==
==About this Structure==
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Revision as of 20:19, 2 July 2008

Image:1m6o.png

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

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