Cited by 81Protein Structure and DynamicsGenomics and Phylogenetic StudiesEvolution and Genetic Dynamics

Inter-residue, inter-protein and inter-family coevolution: bridging the scales

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Szurmant, Hendrik, Weigt, Martin·2018·Current Opinion in Structural Biology

Abstract

Interacting proteins coevolve at multiple but interconnected scales, from the residue-residue over the protein-protein up to the family-family level. The recent accumulation of enormous amounts of sequence data allows for the development of novel, data-driven computational approaches. Notably, these approaches can bridge scales within a single statistical framework. Although being currently applied mostly to isolated problems on single scales, their immense potential for an evolutionary informed, structural systems biology is steadily emerging.

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Crossref · 10.1016/j.sbi.2017.10.014

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  • More recent methods incorporate inter-protein residue-residue contact predictions obtained via co-evolutionary analysis and a deep learning algorithm.

    “More recent methods incorporate inter-protein residue-residue contact predictions obtained via co-evolutionary analysis17 and a deep learning algorithm18.”

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  1. [49]Rose PW Prlic A Altunkaya A Bi C Bradley AR Christie CH Costanzo LD Duarte JM Dutta S Feng Z The RCSB protein data bank: integrative view of protein, gene and 3D structural information Nucleic Acids Res 2017 45 D271 D281 27794042 PMC5210513

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Authors
Szurmant, H., & Weigt, M.
Affiliations
  • Western University of Health Sciences (US)
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Szurmant, Hendrik
  • Weigt, Martin
Venue
Current Opinion in Structural Biology
Publisher
Elsevier BV
Published
2018-06
Volume
50
Pages
26-32
ISSN
0959-440X (ISSN-L)
OpenAlex
W2766246727
Cited by
81
References
53
Citations by year
2026: 4 · 2025: 1 · 2024: 7 · 2023: 8 · 2022: 13 · 2021: 12 · 2020: 10 · 2019: 22 · 2018: 4
FWCI
0.92
Type
journal article
Language
en
Open access
Locations
  • Current Opinion in Structural Biology (acceptedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • arXiv (Cornell University) (submittedVersion)
  • HAL (submittedVersion)
  • arXiv (Cornell University)
Funders
  • Horizon 2020 (GM106085, 734439)
  • National Institute of General Medical Sciences
  • Agence Nationale de la Recherche (ANR-13-BS04-0012-01)
  • National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
Keywords
coevolution, protein-protein interaction, residue-residue interactions, protein families, protein sequence evolution
MeSH terms
Amino Acid Sequence, Amino Acids, Binding Sites, Multigene Family, Models, Molecular, Protein Binding, Protein Conformation, Proteins, Evolution, Molecular, Quantitative Structure-Activity Relationship, Databases, Protein

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