Abstract
Trismus-pseudocamptodactyly (TPS) syndrome is a musculoskeletal disorder, caused by mutation in the perinatal MyH8 gene, leading to the incomplete opening of mouth and camptodactyly of fingers upon dorsiflexion of the wrist. MyH8 gene is relevant for muscle regulation, and it plays a significant role in muscle motor function, the hydrolysis of ATP, that is essential for the production of force for muscle movement. To understand the structural basis of TPS, we utilize a large number of software packages to estimate how the Arg674Gln mutation would affect the structure and stability of MyH8 gene product. The motor domain of MYH8 was modeled in order to know what are the interactions altered in the mutant protein. Further, we docked the ATP in the nucleotide binding region of both wild type and Arg674Gln mutant to understand the mechanism of action. Our strategy may be helpful for understanding the mechanism of regulation of muscle movements and the role of Arg674Gln mutation in TPS.
Keywords: Docking, homology modeling, MyH8 gene, myosin, protein-protein interaction and trismus-pseudocamptodactyly syndrome.
Letters in Drug Design & Discovery
Title:Structural Characterization, Homology Modeling and Docking Studies of ARG674 Mutation in MyH8 Gene Associated with Trismus-Pseudocamptodactyly Syndrome
Volume: 11 Issue: 10
Author(s): Munazzah Tasleem, Romana Ishrat, Asimul Islam, Faizan Ahmad and Md. Imtaiyaz Hassan
Affiliation:
Keywords: Docking, homology modeling, MyH8 gene, myosin, protein-protein interaction and trismus-pseudocamptodactyly syndrome.
Abstract: Trismus-pseudocamptodactyly (TPS) syndrome is a musculoskeletal disorder, caused by mutation in the perinatal MyH8 gene, leading to the incomplete opening of mouth and camptodactyly of fingers upon dorsiflexion of the wrist. MyH8 gene is relevant for muscle regulation, and it plays a significant role in muscle motor function, the hydrolysis of ATP, that is essential for the production of force for muscle movement. To understand the structural basis of TPS, we utilize a large number of software packages to estimate how the Arg674Gln mutation would affect the structure and stability of MyH8 gene product. The motor domain of MYH8 was modeled in order to know what are the interactions altered in the mutant protein. Further, we docked the ATP in the nucleotide binding region of both wild type and Arg674Gln mutant to understand the mechanism of action. Our strategy may be helpful for understanding the mechanism of regulation of muscle movements and the role of Arg674Gln mutation in TPS.
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Cite this article as:
Tasleem Munazzah, Ishrat Romana, Islam Asimul, Ahmad Faizan and Hassan Imtaiyaz Md., Structural Characterization, Homology Modeling and Docking Studies of ARG674 Mutation in MyH8 Gene Associated with Trismus-Pseudocamptodactyly Syndrome, Letters in Drug Design & Discovery 2014; 11 (10) . https://dx.doi.org/10.2174/1570180811666140717190217
DOI https://dx.doi.org/10.2174/1570180811666140717190217 |
Print ISSN 1570-1808 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-628X |
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