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Three-dimensional structure model and predicted ATP interaction rewiring of a deviant RNA ligase 2

Author(s): Sandrine Moreira

CONCLUSION: Homology modeling and molecular dynamics simulations strongly suggest that DpRNL is an RNA ligase 2. The predicted innovative reshaping of DpRNL's catalytic pocket is worthwhile to be tested experimentally.

Article GUID: 26449279
Title:Three-dimensional structure model and predicted ATP interaction rewiring of a deviant RNA ligase 2
Authors:Sandrine Moreira
Link:https://pubmed.ncbi.nlm.nih.gov/26449279/
DOI:10.1186/s12900-015-0046-0
Category:
PMID:26449279
Dept Affiliation: CERMM
1 Department of Biochemistry and Robert-Cedergren Centre for Bioinformatics and Genomics, Université de Montréal, Montreal, QC, Canada. sandrine.moreira@umontreal.ca.
2 Department of Biochemistry, currently Département d'informatique et de recherche opérationnelle (DIRO), Université de Montréal, Montreal, QC, Canada. fmr.noutahi@umontreal.ca.
3 Department of Chemistry and Biochemistry, Centre for Research in Molecular Modeling (CERMM), Groupe d'étude des protéines membranaires (GÉPROM), Regroupement québécois de recherche sur la fonction, l'ingénierie et les applications des protéines (PROTEO), Concordia University, Montreal, QC, Canada. Guillaume.Lamoureux@concordia.ca.
4 Department of Biochemistry and Robert-Cedergren Centre for Bioinformatics and Genomics, Université de Montréal, Montreal, QC, Canada. gertraud.burger@umontreal.ca.

Description:

CONCLUSION: Homology modeling and molecular dynamics simulations strongly suggest that DpRNL is an RNA ligase 2. The predicted innovative reshaping of DpRNL's catalytic pocket is worthwhile to be tested experimentally.