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Article

Molecular dynamics study of enhanced autophosphorylation by S904F mutation of the RET kinase domain.

Journal of structural biology - 1 Dec 2021

Chen Ya-Jyun, Li Pei-Yi, Yang Chia-Ning

Abstract excerpt

The aberrant kinase activity of RET (rearranged during transfection), a transmembrane tyrosine kinase, is associated with human cancer. A point mutation caused by the replacement of solvent-front hydrophilic S904, located on the activation loop (A-loop), with a bulky hydrophobic phenylalanine residue can induce resistance to the type I kinase inhibitor vandetanib. A possible mechanism of this drug resistance is...

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PMID: 34563653
DOI: 10.1016/j.jsb.2021.107799

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