Structural Characterization, Homology Modeling and Docking Studies of ARG674 Mutation in MyH8gene Associated with Trismus-Pseudocamptodactyly Syndrome

ISSN: 1875-628X (Online)
ISSN: 1570-1808 (Print)


Volume 11, 10 Issues, 2014


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Structural Characterization, Homology Modeling and Docking Studies of ARG674 Mutation in MyH8gene Associated with Trismus-Pseudocamptodactyly Syndrome

Author(s): Munazzah Tasleem, Romana Ishrat, Asimul Islam, Faizan Ahmad and Md. Imtaiyaz Hassan

Affiliation: Centre for Interdisciplinary Research In Basic Sciences Jamia Millia Islamia, Jamia Nagar New Delhi 10025, INDIA.

Abstract

Trismus-pseudocamptodactyly (TPS) syndrome is a musculoskeletal disorder, caused by mutation in the perinatal MyH8 gene, leading to the incomplete opening of the 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 then homology modeled in order to infer what amino acid interactions would be altered in the mutant protein. Further, we docked the ATP in the nucleotide binding region of both wild type and Arg674Gln mutant. 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

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Article Details

Volume: 11
First Page: 1
Last Page: 11
Page Count: 11
DOI: 10.2174/1570180811666140717190217
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