Allosteric cross-talk between the hydrophobic cleft and the BH4 domain of Bcl-2 in control of inositol 1,4,5-trisphosphate receptor activity.

George Shapovalov Abigaël Ritaine Nadege Charlene Essonghe Ian de RidderHristina IvanovaSpyridoula Karamanou Anastassios Economou Geert Bultynck Roman Skryma Natalia Prevarskaya

Published in: Exploration of targeted anti-tumor therapy (2022)

R activity, leading to Bcl-2 rebinding with smaller affinity and lesser inhibitory effect. MDs simulations of free and ABT-199 bound Bcl-2 propose a molecular model of such disruption, involving an allosteric interaction with the BH4 domain on the opposite side of Bcl-2.

Keyphrases

small molecule
molecular dynamics
ionic liquid
mass spectrometry
binding protein