Origin, structure and motifs of naturally processed MHC class II ligands

In the past few years a considerable number of naturally processed MHC class II ligands have been identified and sequenced. Most of them derive from endogenous sources, predominantly from plasma membrane proteins. Generally, they display variability in length but exhibit characteristic patterns of i...

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Veröffentlicht in:	Current opinion in immunology 1994-02, Vol.6 (1), p.45-51
Hauptverfasser:	Rötzschke, Olaf, Falk, Kirsten
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Biological Evolution Epitopes - immunology Histocompatibility Antigens Class II - genetics Histocompatibility Antigens Class II - immunology Humans Ligands Molecular Sequence Data Peptides - chemistry Peptides - immunology
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creator	Rötzschke, Olaf Falk, Kirsten
description	In the past few years a considerable number of naturally processed MHC class II ligands have been identified and sequenced. Most of them derive from endogenous sources, predominantly from plasma membrane proteins. Generally, they display variability in length but exhibit characteristic patterns of invariant amino acid positions, which reflect the allele-specific binding requirements. As a general feature, class II ligands also often contain a pattern of proline residues interpreted as a ‘processing motif’.
doi_str_mv	10.1016/0952-7915(94)90032-9
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subjects	Amino Acid Sequence Animals Binding Sites Biological Evolution Epitopes - immunology Histocompatibility Antigens Class II - genetics Histocompatibility Antigens Class II - immunology Humans Ligands Molecular Sequence Data Peptides - chemistry Peptides - immunology
title	Origin, structure and motifs of naturally processed MHC class II ligands
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