Disrupting enzyme fluidity

A combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton’s tyrosine kinase and alter the conformation of this enzyme.

Bibliographic Details
Main Author: Ganesh Srinivasan Anand
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2021-01-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/65221
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author Ganesh Srinivasan Anand
author_facet Ganesh Srinivasan Anand
author_sort Ganesh Srinivasan Anand
collection DOAJ
description A combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton’s tyrosine kinase and alter the conformation of this enzyme.
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spelling doaj.art-6d5b7c8f5baf46aea5ae0b6d3a9aad0b2022-12-22T04:29:19ZengeLife Sciences Publications LtdeLife2050-084X2021-01-011010.7554/eLife.65221Disrupting enzyme fluidityGanesh Srinivasan Anand0https://orcid.org/0000-0001-8995-3067Department of Chemistry and Huck Institute of Life Sciences, Pennsylvania State University, University Park, United StatesA combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton’s tyrosine kinase and alter the conformation of this enzyme.https://elifesciences.org/articles/65221bruton tyrosine kinasekinase inhibitordrug resistanceallosteryhydrogen/deuterium exchange mass spectrometrynuclear magnetic resonance
spellingShingle Ganesh Srinivasan Anand
Disrupting enzyme fluidity
eLife
bruton tyrosine kinase
kinase inhibitor
drug resistance
allostery
hydrogen/deuterium exchange mass spectrometry
nuclear magnetic resonance
title Disrupting enzyme fluidity
title_full Disrupting enzyme fluidity
title_fullStr Disrupting enzyme fluidity
title_full_unstemmed Disrupting enzyme fluidity
title_short Disrupting enzyme fluidity
title_sort disrupting enzyme fluidity
topic bruton tyrosine kinase
kinase inhibitor
drug resistance
allostery
hydrogen/deuterium exchange mass spectrometry
nuclear magnetic resonance
url https://elifesciences.org/articles/65221
work_keys_str_mv AT ganeshsrinivasananand disruptingenzymefluidity