title: Evolution driven structural changes in CENP-E motor domain.
abstract: Genetic evolution corresponds to various biochemical changes that are vital development of new functional traits. Phylogenetic analysis has provided an important insight into the genetic closeness among species and their evolutionary relationships. Centromere-associated protein-E (CENP-E) protein is vital for maintaining cell cycle and checkpoint signal mechanisms are vital for recruitment process of other essential kinetochore proteins. In this study we have focussed on the evolution driven structural changes in CENP-E motor domain among primate lineage. Through molecular dynamics simulation and computational chemistry approaches we examined the changes in ATP binding affinity and conformational deviations in human CENP-E motor domain as compared to the other primates. Root mean square deviation (RMSD), Root mean square fluctuation (RMSF), Radius of gyration (Rg) and principle component analysis (PCA) results together suggested a gain in stability level as we move from tarsier towards human. This study provides a significant insight into how the cell cycle proteins and their corresponding biochemical activities are evolving and illustrates the potency of a theoretical approach for assessing, in a single study, the structural, functional, and dynamical aspects of protein evolution.
authors.affiliation: Bioinformatics Division, School of Bio Sciences and Technology, Vellore Institute of Technology University, Vellore 632014, Tamil Nadu, India.
authors.forename: Ambuj
authors.initials: A
authors.lastname: Kumar
authors.forename: Balu
authors.initials: B
authors.lastname: Kamaraj
authors.forename: Rao
authors.initials: R
authors.lastname: Sethumadhavan
authors.forename: Rituraj
authors.initials: R
authors.lastname: Purohit
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000235:genetics*; D019143:Evolution, Molecular; D006801:Humans; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000235:genetics*; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013816:Thermodynamics; D013997:Time Factors
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D020409:Molecular Motor Proteins; C068688:centromere protein E