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.
Export Options
About this article
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 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Antagonists of Growth Hormone-Releasing Hormone in Oncology
Combinatorial Chemistry & High Throughput Screening CCR5 as a Potential Target in Cancer Therapy: Inhibition or Stimulation?
Anti-Cancer Agents in Medicinal Chemistry Somatostatin and Octreotide on the Treatment of Acute Pancreatitis - Basic and Clinical Studies for Three Decades
Current Pharmaceutical Design Proteome Adjustments Post Gradual Hypoxic Stress in Barilius bendelisis: Insights into Adaptive Strategies of a Hill Stream Cyprinid
Current Proteomics Angiotensin II Receptor Blocker: Possibility of Antitumor Agent for Prostate Cancer
Mini-Reviews in Medicinal Chemistry Relationships between Serotoninergic System and Skin Fibrotic
Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry CD26/Dipeptidyl Peptidase IV as a Novel Therapeutic Target for Cancer and Immune Disorders
Mini-Reviews in Medicinal Chemistry Peptides as Therapeutic Agents or Drug Leads for Autoimmune, Hormone Dependent and Cardiovascular Diseases
Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry Is Technical-Grade Chlordane an Obesogen?
Current Medicinal Chemistry Novobiocin Analogs as Potential Anticancer Agents
Mini-Reviews in Medicinal Chemistry Polyphenols in Disease: from Diet to Supplements
Current Pharmaceutical Biotechnology Small Heat Shock Proteins and the Endoplasmic Reticulum: Potential Attractive Therapeutic Targets?
Current Molecular Medicine Insights into the Structural Features Essential for JAK2 Inhibition and Selectivity
Current Medicinal Chemistry Biomaterial and Mesenchymal Stem Cell for Articular Cartilage Reconstruction
Current Stem Cell Research & Therapy Modulators of Voltage-Dependent Calcium Channels for the Treatment of Nervous System Diseases
Recent Patents on CNS Drug Discovery (Discontinued) Adiponectin: Merely a Bystander or the Missing Link to Cardiovascular Disease?
Current Topics in Medicinal Chemistry Synthesis, Biological and Computational Evaluation of Novel 2,3-dihydro-2-aryl-4-(4- isobutylphenyl)-1,5-benzothiazepine Derivatives as Anticancer and Anti-EGFR Tyrosine Kinase Agents
Anti-Cancer Agents in Medicinal Chemistry Cancer Gene Therapy by Adenovirus-Mediated Gene Transfer
Current Gene Therapy DNA Vaccination in Oncology: Current Status, Opportunities and Perspectives
Current Clinical Pharmacology Meet Our Editorial Board Member:
Anti-Cancer Agents in Medicinal Chemistry