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MHC class II function preserved by low-affinity peptide interactions preceding stable binding.

Abstract：

:Major histocompatibility complex class II molecules and their peptide ligands show unusual interaction kinetics, with slow association and dissociation rates that yield an apparent equilibrium constant of approximately 10(-6)-10(-8) M (refs 1-5). However, there is evidence for a specific, rapidly formed, short-lived complex. The altered migration on SDS-polyacrylamide gel electrophoresis of class II molecules upon stable peptide binding has led to the hypothesis that the two kinetically distinguishable types of class II-peptide complexes correspond to different structures. In accord with this model, we demonstrate here that insect cell-derived HLA-DR1 class II molecules show fast, almost stoichiometric occupancy with rapidly dissociating peptide while remaining sensitive to SDS-induced chain dissociation. The same DR1 molecules slowly and quantitatively form long-lived complexes resistant to SDS-induced denaturation. Surprisingly, low-affinity interaction with peptide protects class II from denaturation at physiological temperature, a finding that has implications for understanding the role of invariant chain in the intracellular behaviour of class II molecules.

journal_name

Nature

journal_title

Nature

authors

Sadegh-Nasseri S,Stern LJ,Wiley DC,Germain RN

doi

10.1038/370647a0

subject

Has Abstract

pub_date

1994-08-25 00:00:00

pages

647-50

issue

6491

eissn

0028-0836

issn

1476-4687

journal_volume

370

pub_type

杂志文章

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