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Unique methionine-aromatic interactions govern the calmodulin redox sensor.

Abstract：

:Calmodulin contains multiple redox sensitive methionines whose oxidation alters the regulation of numerous targets. Molecular dynamics simulations were used to define the molecular principles that govern how calmodulin is structurally poised to detect and respond to methionine oxidation. We found that calmodulin's open and closed states were preferentially stabilized by unique, redox sensitive, methionine-aromatic interactions. Key methionine-aromatic interactions were coupled to reorientation of EF hand helices. Methionine to glutamine substitutions designed to mimic methionine oxidation strongly altered conformational transitions by modulating the strength of methionine-aromatic interactions. Together, these results suggest a broadly applicable redox sensing mechanism though which methionine oxidation by cellular oxidants alters the strength of methionine-aromatic interactions critical for functional protein dynamics.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Walgenbach DG,Gregory AJ,Klein JC

doi

10.1016/j.bbrc.2018.09.052

subject

Has Abstract

pub_date

2018-10-20 00:00:00

pages

236-241

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)31970-3

journal_volume

505

pub_type

杂志文章

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