Competition between Intradomain and Interdomain Interactions: A Buried Salt Bridge Is Essential for Villin Headpiece Folding and Actin Binding
Author:
Affiliation:
1. Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118, United States
2. Department of Chemistry, State University of New York, Stony Brook, New York 11794, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1020343
Reference37 articles.
1. Isolation of a domain of villin retaining calcium-dependent interaction with G-actin, but devoid of F-actin fragmenting activity
2. The 3D Structure of Villin as an Unusual F-Actin Crosslinker
3. NMR structure of an F-actin-binding “headpiece” motif from villin
4. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
5. Cysteine Scanning Mutagenesis at 40 of 76 Positions in Villin Headpiece Maps the F-Actin Binding Site and Structural Features of the Domain
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1. Plant Villin Headpiece Domain Demonstrates a Novel Surface Charge Pattern and High Affinity for F-Actin;Biochemistry;2018-02-14
2. Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization;Protein Science;2016-07-04
3. Protein Conformational Dynamics and Signaling in Evolution and Pathophysiology;Biased Signaling in Physiology, Pharmacology and Therapeutics;2014
4. Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein;Protein Science;2013-12-03
5. On the unyielding hydrophobic core of villin headpiece;Protein Science;2012-03-30
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