B-POCKET TRANSPLANT FROM HLA-A2 INTO B27 CHANGES REQUIREMENT FOR P-2 ANCHOR RESIDUE IN PEPTIDE PRESENTATION

B-POCKET TRANSPLANT FROM HLA-A2 INTO B27 CHANGES REQUIREMENT FOR P-2 ANCHOR RESIDUE IN PEPTIDE PRESENTATION

Manylion Llyfryddiaeth
Prif Awduron:	Colbert, R, Rowlandjones, S, Mcmichael, A, Frelinger, J
Fformat:	Journal article
Cyhoeddwyd:	1993

Eitemau Tebyg

Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.
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Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.
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Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides.
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An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide.
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ERAP2 is associated with ankylosing spondylitis in HLA-B27-positive and HLA-B27-negative patients.
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HLA-B27
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HLA-B27 transgenic rodents express cell surface HLA-B27 heavy chain homodimers and multimers.
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Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility
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