Subasri, S and Chaudhary, SK and Kesharwani, M and Sekar, K and Velmurugan, D (2022) Missense mutations in fumarate hydratase leading to cancer: Molecular modeling and molecular dynamics simulations of the mutants. [Book Chapter]
Full text not available from this repository.Abstract
Mutations in fumarase hydratase (FH) which affect the hydrogen bond interactions with active site residues lead to multiple cutaneous and uterine leiomyomatosis and hereditary leiomyomatosis and renal cell cancer(RCC). R233 mutation is reported as the most commonly described FH mutation and it has been associated with RCC. This negative dominant mutation might affect the active site without affecting the overall three-dimensional structure, or could exhibit effects on the overall structure resulting in misfolding. Modeling studies carried out with R233H mutation showed the loss of interaction with E355. Also, the K230R mutation leads to the loss of interaction with E355. E355K mutation is found to lead to the loss of interaction with K230 and R233. Molecular dynamics simulations studies show that the mutation in R233 to H233 causes loss of structural integrity in the active site of FH structure. © 2023 by World Scientific Publishing Co. Pte. Ltd.
| Item Type: | Book Chapter |
|---|---|
| Publication: | Therapeutic Protein Targets For Drug Discovery And Clinical Evaluation: Bio-crystallography And Drug Design |
| Publisher: | World Scientific Publishing Co. |
| Additional Information: | The copyright for this article belongs to World Scientific Publishing Co. |
| Department/Centre: | Division of Interdisciplinary Sciences > Computational and Data Sciences Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 09 Jan 2023 06:55 |
| Last Modified: | 09 Jan 2023 06:55 |
| URI: | https://eprints.iisc.ac.in/id/eprint/78903 |
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