Peptide interaction with a class I major histocompatibility complex-encoded molecule: allosteric control of the ternary complex stability

Biochemistry
D M GakamskyI Pecht

Abstract

Thermodynamics and kinetics of interaction between a soluble class I MHC heterodimer composed of the H-2Kd heavy chain (H) and human beta 2microglobulin (beta 2m) with a dansylated peptide series based on residues 147-155 of influenza virus nucleoprotein sequence were studied by means of real-time fluorescence measurements. Peptide-heterodimer binding is a second-order process with specific rates practically independent of peptide structure (3-5 x 10(6) M-1 s-1). The ternary complex assembly involves a rate-limiting step of beta 2m association with H to yield an unstable heterodimer (tau < or = 5 s, 37 degrees C). Peptide binding provides a positive feedback enhancing H's affinity for beta 2m, thus stabilizing the ternary complex. The latter decays by either peptide or beta 2m dissociation. The first-order rate constants of peptide dissociation (0.5 x 10(-2))-(0.4 x 10(-3)) s-1, 37 degrees C) depend on their structures and are faster than that of beta 2m dissociation. The former process decreases the H affinity for beta 2m and induces their dissociation. This dissociation, in turn, drastically lowers H affinity for peptide. Thus, these three components produce a system which is stable as a trimer. This behavior is rationalized ...Continue Reading

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Citations

Apr 7, 2004·Journal of Molecular Biology·Paula M Petrone, Angel E Garcia
Mar 10, 2012·Proceedings of the National Academy of Sciences of the United States of America·Herman N EisenRichard J Cohen
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Jun 20, 2021·The Journal of Immunology : Official Journal of the American Association of Immunologists·Yanan WuChun Xia

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