An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39-Reference-Cited by-同舟云学术

An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39

Published:2000-06-12 Issue:12 Volume:191 Page:2083-2092
ISSN:0022-1007
Container-title:Journal of Experimental Medicine
language:en
Short-container-title:

Author:

Yagüe Jesús¹,Alvarez Iñaki¹,Rognan Didier²,Ramos Manuel¹,Vázquez Jesús¹,de Castro José A. López¹

Affiliation:

1. Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Facultad de Ciencias, 28049 Madrid, Spain

2. Department of Applied Biosciences, Eidgenössiche Technische Hochschule, CH-8057 Zürich, Switzerland

Abstract

Sequence-independent interactions involving the free peptidic NH2 terminus are thought to be an essential feature of peptide binding to classical major histocompatibility complex (MHC) class I proteins. Challenging this paradigm, a natural Nα-acetylated ligand of human histocompatibility leukocyte antigen (HLA)-B39 was identified in this study. It matched the NH2-terminal sequence of two human helicases, was resistant to aminopeptidase M, and was produced with high yield from a synthetic 30 mer with the sequence of the putative parental protein by the 20S proteasome. This is the first reported natural ligand of classical MHC class I antigens that has a blocked NH2 terminus.

Publisher

Rockefeller University Press

Subject

Immunology,Immunology and Allergy

Link

http://rupress.org/jem/article-pdf/191/12/2083/1124871/992244.pdf

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