ArticlePLoS computational biology2017
Unifying view of mechanical and functional hotspots across class A GPCRs.
Article in PLoS computational biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Coevolutionary data-based interaction networks approach highlighting key residues across protein families: The case of the G-protein coupled receptors.Computational and structural biotechnology journal · 2020Article
- Key residues controlling bidirectional ion movements in NaCell calcium · 2018Article
- Structural dynamics is a determinant of the functional significance of missense variants.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) are the largest superfamily of signaling proteins. Their activation process is accompanied by conformational changes that have not yet been fully uncovered. Here, we carry out a novel comparative analysis of internal structural fluctuations across a variety of receptors from class A GPCRs, which currently has the richest structural coverage. We infer the local mechanical couplings underpinning the receptors' functional dynamics and finally identify those amino acids whose virtual deletion causes a significant softening of the mechanical network. The relevance of these amino acids is demonstrated by their overlap with those known to be crucial for GPCR function, based on static structural criteria. The differences with the latter set allow us to identify those sites whose functional role is more clearly detected by considering dynamical and mechanical properties. Of these sites with a genuine mechanical/dynamical character, the top ranking is amino acid 7x52, a previously unexplored, and experimentally verifiable key site for GPCR conformational response to ligand binding.
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