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Self-release of CLIP in peptide loading of HLA-DR molecules.

Self-release of CLIP in peptide loading of HLA-DR molecules. The assembly and transport of major histocompatibility complex (MHC) class II molecules require interaction with the invariant chain. A fragment of the invariant chain, CLIP, occupies the peptide-binding groove of the class II molecule. At endosomal pH, the binding of CLIP to human MHC class II HLA-DR molecules was counteracted by its amino-terminal segment (residues 81 to 89), which facilitated rapid release. The CLIP (81-89) fragment also catalyzed the release of CLIP(90-105) and a subset of other self-peptides, probably by transient interaction with an effector site outside the groove. Thus, CLIP may facilitate peptide loading through an allosteric release mechanism. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Science (New York, N.Y.) Pubmed

Self-release of CLIP in peptide loading of HLA-DR molecules.

Kropshofer, H; Vogt, A B; Stern, L J; Hämmerling, G J
Science (New York, N.Y.) , Volume 270 (5240): -1347 – Dec 28, 1995
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Self-release of CLIP in peptide loading of HLA-DR molecules.


Abstract

The assembly and transport of major histocompatibility complex (MHC) class II molecules require interaction with the invariant chain. A fragment of the invariant chain, CLIP, occupies the peptide-binding groove of the class II molecule. At endosomal pH, the binding of CLIP to human MHC class II HLA-DR molecules was counteracted by its amino-terminal segment (residues 81 to 89), which facilitated rapid release. The CLIP (81-89) fragment also catalyzed the release of CLIP(90-105) and a subset of other self-peptides, probably by transient interaction with an effector site outside the groove. Thus, CLIP may facilitate peptide loading through an allosteric release mechanism.

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ISSN
0036-8075
DOI
10.1126/science.270.5240.1357
pmid
7481823

Abstract

The assembly and transport of major histocompatibility complex (MHC) class II molecules require interaction with the invariant chain. A fragment of the invariant chain, CLIP, occupies the peptide-binding groove of the class II molecule. At endosomal pH, the binding of CLIP to human MHC class II HLA-DR molecules was counteracted by its amino-terminal segment (residues 81 to 89), which facilitated rapid release. The CLIP (81-89) fragment also catalyzed the release of CLIP(90-105) and a subset of other self-peptides, probably by transient interaction with an effector site outside the groove. Thus, CLIP may facilitate peptide loading through an allosteric release mechanism.

Journal

Science (New York, N.Y.) – Pubmed

Published: Dec 28, 1995

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