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Toggling of Diacylglycerol Affinity Correlates with Conformational Plasticity in C1 Domains. | LitMetric

Toggling of Diacylglycerol Affinity Correlates with Conformational Plasticity in C1 Domains.

Biochemistry

Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.

Published: May 2017

AI Article Synopsis

Article Abstract

Conserved homology-1 (C1) domains are peripheral membrane domains that target their host proteins to diacylglycerol (DAG)-containing membranes. It has been previously shown that a conservative aromatic mutation of a single residue in the C1 domain has a profound effect on DAG affinity. We report that the "DAG-toggling" mutation changes the conformational dynamics of the loop region that forms the binding site for the C1 activators. Moreover, there is a correlation among the residue identity at the mutation site, DAG affinity, and loop dynamics in four C1 variants. We propose that "toggling" of DAG affinity may occur through modulation of both protein-membrane interactions and the geometry of the activator-binding cleft, with the loop dynamics being responsible for the latter.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5600822PMC
http://dx.doi.org/10.1021/acs.biochem.7b00228DOI Listing

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