An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo

Sequence-independent interactions involving the free peptidic NH(2) 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...

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Autores principales: Yagüe, Jesús, Alvarez, Iñaki, Rognan, Didier, Ramos, Manuel, Vázquez, Jesús, de Castro, José A. López
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193201/
https://www.ncbi.nlm.nih.gov/pubmed/10859333
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author Yagüe, Jesús
Alvarez, Iñaki
Rognan, Didier
Ramos, Manuel
Vázquez, Jesús
de Castro, José A. López
author_facet Yagüe, Jesús
Alvarez, Iñaki
Rognan, Didier
Ramos, Manuel
Vázquez, Jesús
de Castro, José A. López
author_sort Yagüe, Jesús
collection PubMed
description Sequence-independent interactions involving the free peptidic NH(2) 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 NH(2)-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 NH(2) terminus.
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spelling pubmed-21932012008-04-16 An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo Yagüe, Jesús Alvarez, Iñaki Rognan, Didier Ramos, Manuel Vázquez, Jesús de Castro, José A. López J Exp Med Original Article Sequence-independent interactions involving the free peptidic NH(2) 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 NH(2)-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 NH(2) terminus. The Rockefeller University Press 2000-06-19 /pmc/articles/PMC2193201/ /pubmed/10859333 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Yagüe, Jesús
Alvarez, Iñaki
Rognan, Didier
Ramos, Manuel
Vázquez, Jesús
de Castro, José A. López
An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title_full An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title_fullStr An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title_full_unstemmed An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title_short An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh(2) Terminus in Vivo
title_sort n-acetylated natural ligand of human histocompatibility leukocyte antigen (hla)-b39: classical major histocompatibility complex class i proteins bind peptides with a blocked nh(2) terminus in vivo
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193201/
https://www.ncbi.nlm.nih.gov/pubmed/10859333
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