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Overall, we suggest that phosphotyrosyl ligand binding causes conformational changes in the SH3-SH2 and βB- βC linkers, part of the βD, and βD-βE linker region, thereby allowing for modulation of kinase activity.
However, the integrin system offers a possible explanation of how ligand binding causes conformational changes within a MIDAS domain [64,74].
This binding causes conformational changes of p53 that reduces the p53-MDM2 interandion and hence decreases p53 ubiquitination which then leads to p53 accumulation, MDM2 downregulation, and p53-dependent apoptotic pathway induction [ 65].
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Both protonation and Z binding cause conformational changes that are involved in the thermal dissipation, which can be quantified by measuring nonphotochemical quenching of chlorophyll fluorescence (NPQ) [3].
In canonical mechanism, ligand binding to PPARs causes conformational changes in the receptor, which release corepressor and recruit coactivator.
However, we can not exclude that IκB binding to one partner causes conformational changes (such as a slight change in the curvature of the ankyrin repeats) that affect allosterically the (distant) binding site of the other partner.
For example, in rodent and human Crk, binding of Crk to Abl causes conformational changes that expose a PPPP motif in the Crk SH2 domain that in turn binds the SH3 domain of Abl to stabilize the Abl/Crk interaction [ 167, 168].
Ligand binding to the extracellular α subunit causes conformational changes in the IGF-1R, which activate the tyrosine kinase domain of the intracellular β subunit.
Photoactivation of rhodopsin causes conformational changes that provide a binding site for the rod G protein called transducin.
Doxycycline nonselectively inhibits MMPs by binding to the active zinc sites and also by binding to an inactive calcium site, which causes conformational change and loss of enzymatic activity [ 14].
Taken together, our results suggest that the formation of heterodimers between CXCR4 and CCR5 is a dynamic process and that ligand binding may cause conformational changes in pre-existing CXCR4 CCR5 dimers, destabilize CXCR4 CCR5STA heterodimers or promote CXCR4 CCR5Δ4 heterodimer formation.
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