title: Modeling the mutational effects on calmodulin structure: prediction of alteration in the amino acid interactions.
abstract: Calmodulin (CaM) is a highly conserved 17kDa eukaryotic protein that can bind specifically to over 100 protein targets in response to a Ca2+ signal. Present study was planned to mutate the crucial residues of N-terminal lobe, central helix, and C-terminal lobe that play important roles in activating and binding of enzymes. In all, 10 mutations were carried out in the predicted 3D structure of calmodulin using the computer program MODELLER 6v2. Mutations at specific residues in both the N-terminal and C-terminal regions resulted in the change in the interaction pattern of these amino acids. No significant change was however predicted by mutating amino acid residues in the central helix. The predicted alteration in the interaction of specific amino acids may either alter the binding affinity with calcium ions or decrease the ability of calmodulin to activate the specific enzymes.
authors.affiliation: Department of Pathology, Fatima Jinnah Medical College, Lahore, Pakistan.
authors.forename: Asma
authors.initials: A
authors.lastname: Rashid
authors.forename: Rukhshan
authors.initials: R
authors.lastname: Khurshid
authors.forename: Mumtaz
authors.initials: M
authors.lastname: Begum
authors.lastname: Gul-e-Raana
authors.forename: Mohd
authors.initials: M
authors.lastname: Latif
authors.forename: Asmat
authors.initials: A
authors.lastname: Salim
mesh_terms: D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry*; D001665:Binding Sites; D002147:Calmodulin / Q000737:chemistry*; D003198:Computer Simulation; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D002147:Calmodulin