Molecular Evolution of Protein Conformational Changes Revealed by a Network of Evolutionarily Coupled Residues
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- Title
- Molecular Evolution of Protein Conformational Changes Revealed by a Network of Evolutionarily Coupled Residues
- Authors
- Jeon, J; Nam, HJ; Choi, YS; Yang, JS; Hwang, J; Kim, S
- Date Issued
- 2011-09
- Publisher
- OXFORD UNIV PRESS
- Abstract
- An improved understanding of protein conformational changes has broad implications for elucidating the mechanisms of various biological processes and for the design of protein engineering experiments. Understanding rearrangements of residue interactions is a key component in the challenge of describing structural transitions. Evolutionary properties of protein sequences and structures are extensively studied; however, evolution of protein motions, especially with respect to interaction rearrangements, has yet to be explored. Here, we investigated the relationship between sequence evolution and protein conformational changes and discovered that structural transitions are encoded in amino acid sequences as coevolving residue pairs. Furthermore, we found that highly coevolving residues are clustered in the flexible regions of proteins and facilitate structural transitions by forming and disrupting their interactions cooperatively. Our results provide insight into the evolution of protein conformational changes and help to identify residues important for structural transitions.
- Keywords
- protein sequence evolution; coevolution; protein structure; protein motion; MULTIPLE SEQUENCE ALIGNMENTS; FIXJ RECEIVER DOMAIN; CORRELATED MUTATIONS; CRYSTAL-STRUCTURE; ALLOSTERIC COMMUNICATION; INTRINSIC MOTIONS; NMR-SPECTROSCOPY; ENZYME DYNAMICS; LOCAL MOTIONS; RAS P21
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/17073
- DOI
- 10.1093/MOLBEV/MSR094
- ISSN
- 0737-4038
- Article Type
- Article
- Citation
- MOLECULAR BIOLOGY AND EVOLUTION, vol. 28, no. 9, page. 2675 - 2685, 2011-09
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