DIFFERENCES IN PEPTIDE PRESENTATION BETWEEN B27 SUBTYPES - THE IMPORTANCE OF THE P1 SIDE-CHAIN IN MAINTAINING HIGH-AFFINITY PEPTIDE BINDING TO B-ASTERISK-2703

DIFFERENCES IN PEPTIDE PRESENTATION BETWEEN B27 SUBTYPES - THE IMPORTANCE OF THE P1 SIDE-CHAIN IN MAINTAINING HIGH-AFFINITY PEPTIDE BINDING TO B-ASTERISK-2703

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Colbert, R, Rowlandjones, S, Mcmichael, A, Frelinger, J
التنسيق:	Journal article
منشور في:	1994

مواد مشابهة

Differences in peptide presentation between B27 subtypes: the importance of the P1 side chain in maintaining high affinity peptide binding to B*2703.
حسب: Colbert, R, وآخرون
منشور في: (1994)

B-POCKET TRANSPLANT FROM HLA-A2 INTO B27 CHANGES REQUIREMENT FOR P-2 ANCHOR RESIDUE IN PEPTIDE PRESENTATION
حسب: Colbert, R, وآخرون
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Biological effect of varying peptide binding affinity to the <it>BoLA-DRB3*2703 </it>allele
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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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Distinct recognition of closely-related HIV-1 and HIV-2 cytotoxic T-cell epitopes presented by HLA-B*2703 and B*2705.
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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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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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IMMUNOGENIC HIV VARIANT PEPTIDES THAT BIND TO HLA-B8 BUT FAIL TO STIMULATE CYTOTOXIC T-LYMPHOCYTE RESPONSES
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Significance of the six peptide-binding pockets of HLA-A2.1 in influenza A matrix peptide-specific cytotoxic T-lymphocyte reactivity.
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Evidence of widespread binding of HLA class I molecules to peptides.
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Structural homologies between two HLA B27-restricted peptides suggest residues important for interaction with HLA B27.
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HLA-B27-RESTRICTED PEPTIDE PRESENTATION TO CYTOTOXIC T-CELLS IN REACTIVE ARTHRITIS
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HLA class I typing by PCR: HLA-B27 and an African B27 subtype.
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Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27.
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HLA-A2 subtypes are functionally distinct in peptide binding and presentation.
حسب: Barouch, D, وآخرون
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Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.
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IDENTIFICATION OF T-CELL RECEPTOR RECOGNITION RESIDUES FOR AN INFLUENZA-VIRUS NONAMER PEPTIDE EPITOPE PRESENTED BY HLA B27
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Analysis of mutant HLA-A2 molecules. Differential effects on peptide binding and CTL recognition.
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Interaction of HLA-B27 homodimers with KIR3DL1 and KIR3DL2, unlike HLA-B27 heterotrimers, is independent of the sequence of bound peptide.
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