ArticleBiophysical journal2010
Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Large-Scale AI-Based Structure and Activity Prediction Analysis of ShK Domain Peptides from Sea Anemones in the South China Sea.Marine drugs · 2025Article
- Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Intricacies of Renal Phosphate Reabsorption-An Overview.International journal of molecular sciences · 2024Review
- Conformational dynamics of a multidomain protein by neutron scattering and computational analysis.Biophysical journal · 2021Article
- Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transition between protein-like and polymer-like dynamic behavior: Internal friction in unfolded apomyoglobin depends on denaturing conditions.Scientific reports · 2020Article
- Dynamic structure of the full-length scaffolding protein NHERF1 influences signaling complex assembly.The Journal of biological chemistry · 2019Article
- α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.Biophysical journal · 2018Article
- Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics.Journal of molecular biology · 2017Article
- Modulation of hemoglobin dynamics by an allosteric effector.Protein science : a publication of the Protein Society · 2017Article
- Visualizing the nanoscale: protein internal dynamics and neutron spin echo spectroscopy.Current opinion in structural biology · 2017Review
- Thermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase.Scientific reports · 2017Article
- Nanoscale protein domain motion and long-range allostery in signaling proteins- a view from neutron spin echo sprectroscopy.Biophysical reviews · 2015Article
- Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering.The Journal of biological chemistry · 2015Article
- Molecular conformation of the full-length tumor suppressor NF2/Merlin--a small-angle neutron scattering study.Journal of molecular biology · 2014Article
- Role of the VirA histidine autokinase of Agrobacterium tumefaciens in the initial steps of pathogenesis.Frontiers in plant science · 2014Article
- The tails of apical scaffolding proteins EBP50 and E3KARP regulate their localization and dynamics.Molecular biology of the cell · 2013Article
- Ligand-induced dynamic changes in extended PDZ domains from NHERF1.Journal of molecular biology · 2013Article
- Nanoscale protein dynamics: a new frontier for neutron spin echo spectroscopy.The European physical journal. E, Soft matter · 2013Article
- Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
NHERF1 is a multidomain scaffolding protein that assembles signaling complexes, and regulates the cell surface expression and endocytic recycling of a variety of membrane proteins. The ability of the two PDZ domains in NHERF1 to assemble protein complexes is allosterically modulated by the membrane-cytoskeleton linker protein ezrin, whose binding site is located as far as 110 Ångstroms away from the PDZ domains. Here, using neutron spin echo (NSE) spectroscopy, selective deuterium labeling, and theoretical analyses, we reveal the activation of interdomain motion in NHERF1 on nanometer length-scales and on submicrosecond timescales upon forming a complex with ezrin. We show that a much-simplified coarse-grained model suffices to describe interdomain motion of a multidomain protein or protein complex. We expect that future NSE experiments will benefit by exploiting our approach of selective deuteration to resolve the specific domain motions of interest from a plethora of global translational and rotational motions. Our results demonstrate that the dynamic propagation of allosteric signals to distal sites involves changes in long-range coupled domain motions on submicrosecond timescales, and that these coupled motions can be distinguished and characterized by NSE.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.