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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-...

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Hauptverfasser: Kropshofer, Harald (VerfasserIn) , Vogt, Anne B. (VerfasserIn) , Stern, Lawrence J. (VerfasserIn) , Hämmerling, Günter J. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: November 24, 1995
In: Science
Year: 1995, Jahrgang: 270, Heft: 5240, Pages: 1357-1359
ISSN:1095-9203
DOI:10.1126/science.270.5240.1357
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1126/science.270.5240.1357
Verlag, lizenzpflichtig, Volltext: https://www.science.org/doi/10.1126/science.270.5240.1357
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Verfasserangaben:Harald Kropshofer, Anne B. Vogt, Lawrence J. Stern, Günter J. Hämmerling

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520 |a 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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