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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Nadarajan, Saravanan Prabhu Mathew, Sam Deepankumar, Kanagavel Yun, Hyungdon |
| Description | Country affiliation: South Korea Author Affiliation: Nadarajan SP ( School of Biotechnology, Yeungnam University, Gyeongsan, South Korea.) |
| Abstract | Residue-specific incorporation is a technique used to replace natural amino acids with their close structural analogs, unnatural amino acids (UAAs), during protein synthesis. This is achieved by exploiting the substrate promiscuity of the wild type amino acyl tRNA synthetase (AARS) towards the close structural analogs of their cognate amino acids. In the past few decades, seleno-methionine was incorporated into proteins, using the substrate promiscuity of wild type AARSs, to resolve their crystal structures. Later, the incorporation of many UAAs showed that the AARSs are polyspecific to the close structural analogs of their cognate amino acids and that they maintain fidelity for the 19 natural amino acids. This polyspecificity helps to expand the use of this powerful tool to incorporate various UAA residues specifically through in vivo and in vitro approaches. Incorporation of UAAs is expensive, tedious and time-consuming. For the efficient incorporation of UAAs, it is important to screen substrate selectivity prior to their incorporation. As an initial study, using a docking tool, we analyzed the polyspecificity of the methionyl-tRNA synthetases (MetRSs) towards multiple reported and virtually generated methionine analogs. Based on the interaction result of these docking simulations, we predicted the substrate selectivity of the MetRS and the key residues responsible for the recognition of methionine analogs. Similarly, we compared the active site residues of the MetRSs of different species and identified the conserved amino acids in their active sites. Given the close similarity in the active site residues of these systems, we evaluated the polyspecificity of MetRSs. |
| File Format | HTM / HTML |
| ISSN | 10933263 |
| Volume Number | 39 |
| e-ISSN | 18734243 |
| Journal | Journal of Molecular Graphics and Modelling |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-02-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Molecular Biology Computer Simulation Methionine-trna Ligase Chemistry Models, Molecular Catalytic Domain Methionine Analogs & Derivatives Metabolism Molecular Docking Simulation Substrate Specificity Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Computer Graphics and Computer-Aided Design Spectroscopy Materials Chemistry Physical and Theoretical Chemistry |
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