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

• Verfasst von: Kropshofer, Harald [VerfasserIn]
• Verfasst von: Vogt, Anne B. [VerfasserIn]
• Verfasst von: Stern, Lawrence J. [VerfasserIn]
• Verfasst von: Hämmerling, Günter J. [VerfasserIn]
• Titel: Self-release of CLIP in peptide loading of HLA-DR molecules
• Verf.angabe: Harald Kropshofer, Anne B. Vogt, Lawrence J. Stern, Günter J. Hämmerling
• E-Jahr: 1995
• Jahr: November 24, 1995
• Umfang: 3 S.
• Fussnoten: Gesehen am 17.07.2025
• Titel Quelle: Enthalten in: Science
• Ort Quelle: Washington, DC : American Association for the Advancement of Science, 1880
• Jahr Quelle: 1995
• Band/Heft Quelle: 270(1995), 5240, Seite 1357-1359
• ISSN Quelle: 1095-9203
• DOI: doi:10.1126/science.270.5240.1357
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 193102216X

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.