Conformational restriction of the Tyr53 side-chain in the decapeptide HEL[52-61]: effects on binding to MHC-II I-Ak molecule and TCR recognition-Reference-Cited by-同舟云学术

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Conformational restriction of the Tyr53 side-chain in the decapeptide HEL[52-61]: effects on binding to MHC-II I-Ak molecule and TCR recognition

Published:2000-12 Issue:6 Volume:56 Page:398-408
ISSN:1397-002X
Container-title:The Journal of Peptide Research
language:en
Short-container-title:

Author:

Casimir J.R.,Iterbeke K.,Van Den Nest W.,Tourwé D.,Trescol-Biémont M.-C.,Rabourdin-Combe C.,Dumortier H.,Muller S.,Gerlier D.,Paris J.

Publisher

Wiley

Subject

Endocrinology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1034/j.1399-3011.2000.00777.x/fullpdf

Reference45 articles.

1. X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*04101) complexes with a peptide from human collagen II;Dessen;Immunity,1997

2. Structures of an MHC class II molecule with covalently bound single peptides;Fremont;Science,1996

3. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides;Jardetzky;Proc. Natl Acad. Sci. USA,1996

4. The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding;Murthy;Structure,1997

5. Crystal structure of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues;Scott;Immunity,1998

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