ArticleStructure (London, England : 1993)2009
Non-native interactions are critical for mechanical strength in PKD domains.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- As Simple As Possible, but Not Simpler: Exploring the Fidelity of Coarse-Grained Protein Models for Simulated Force Spectroscopy.PLoS computational biology · 2016Article
- Genetic Analysis Reveals a Hierarchy of Interactions between Polycystin-Encoding Genes and Genes Controlling Cilia Function during Left-Right Determination.PLoS genetics · 2016Article
- A polycystin-centric view of cyst formation and disease: the polycystins revisited.Kidney international · 2015Review
- Polycystin-1 Is a Cardiomyocyte Mechanosensor That Governs L-Type Ca2+ Channel Protein Stability.Circulation · 2015Article
- How well does a funneled energy landscape capture the folding mechanism of spectrin domains?The journal of physical chemistry. B · 2013Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein conformational switches: from nature to design.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Review
- Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains.The Journal of biological chemistry · 2010Article
- Complex unfolding kinetics of single-domain proteins in the presence of force.Biophysical journal · 2010Article
- Understanding biology by stretching proteins: recent progress.Current opinion in structural biology · 2010Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Experimental observation has led to the commonly held view that native state protein topology is the principle determinant of mechanical strength. However, the PKD domains of polycystin-1 challenge this assumption: they are stronger than predicted from their native structure. Molecular dynamics simulations suggest that force induces rearrangement to an intermediate structure, with nonnative hydrogen bonds, that resists unfolding. Here we test this hypothesis directly by introducing mutations designed to prevent formation of these nonnative interactions. We find that these mutations, which only moderately destabilize the native state, reduce the mechanical stability dramatically. The results demonstrate that nonnative interactions impart significant mechanical stability, necessary for the mechanosensor function of polycystin-1. Remarkably, such nonnative interactions result from force-induced conformational change: the PKD domain is strengthened by the application of force.
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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.