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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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Detalles Bibliográficos
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:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193201/
https://www.ncbi.nlm.nih.gov/pubmed/10859333
Descripción
Sumario: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.