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. 1995 Oct 10;92(21):9900–9904. doi: 10.1073/pnas.92.21.9900

Direct observation of disordered regions in the major histocompatibility complex class II-associated invariant chain.

A Jasanoff 1, S J Park 1, D C Wiley 1
PMCID: PMC40910  PMID: 7568241

Abstract

Invariant chain (Ii) is a trimeric membrane protein which binds and stabilizes major histocompatibility complex class II heterodimers in the endoplasmic reticulum and lysosomal compartments of antigen-presenting cells. In concert with an intracellular class II-like molecule, HLA-DM, Ii seems to facilitate loading of conventional class II molecules with peptides before transport of the class II-peptide complex to the cell surface for recognition by T cells. The interaction of Ii with class II molecules is thought to be mediated in large part through a region of 24 amino acids (the class II-associated Ii peptide, CLIP) which binds as a cleaved moiety in the antigenic peptide-binding groove of class II molecules in HLA-DM-deficient cell lines. Here we use nuclear magnetic resonance techniques to demonstrate that a soluble recombinant Ii ectodomain contains significant disordered regions which probably include CLIP.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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