@article {47726,
	title = {Water mediated allosteric network in beta 2AR T164I variant modulates agonist binding affinity},
	journal = {European Biophysics Journal with Biophysics Letters},
	volume = {50},
	year = {2021},
	month = {JUL},
	pages = {162},
	type = {Meeting Abstract},
	issn = {0175-7571},
	author = {Nikte, Siddhanta V. and Sonar, Krushna and Tandale, Aditi and Sengupta, Durba and Joshi, Manali}
}
@article {48970,
	title = {State-dependent dynamics of extramembrane domains in the <i>β</i><sub>2</sub>-adrenergic receptor},
	journal = {Proteins- Structure Function and Bioinformatics },
	volume = {92},
	year = {2024},
	month = {MAR},
	pages = {317-328},
	type = {Article},
	abstract = {<p>G protein-coupled receptors (GPCRs) are membrane-bound signaling proteins that play an essential role in cellular signaling processes. Due to their intrinsic function of transmitting internal signals in response to external cues, these receptors are adapted to be highly dynamic in nature. The beta(2)-adrenergic receptor (beta 2AR) is a representative member of the family that has been extensively analyzed in terms of its structure and activation. Although the structure of the transmembrane domain has been characterized in the different functional states of the receptor, the conformational dynamics of the extramembrane domains, especially the intrinsically disordered regions are still emerging. In this study, we analyze the state-dependent dynamics of extramembrane domains of beta(2)AR using atomistic molecular dynamics simulations. We introduce a parameter, the residue excess dynamics that allows us to better quantify receptor dynamics. Using this measure, we show that the dynamics of the extramembrane domains are sensitive to the receptor state. Interestingly, the ligand-bound intermediate R{\textquoteright} state shows the maximal dynamics compared to either the active R*G or inactive R states. Ligand binding appears to be correlated with high residue excess dynamics that are dampened upon G protein coupling. The intracellular loop-3 (ICL3) domain has a tendency to flip towards the membrane upon ligand binding, which could contribute to receptor {\textquoteleft}{\textquoteleft}priming.{\textquoteright}{\textquoteright} We highlight an important ICL1-helix-8 interplay that is broken in the ligand-bound state but is retained in the active state. Overall, our study highlights the importance of characterizing the functional dynamics of the GPCR loop domains.</p>
},
	keywords = {allosteric pathway, beta-2 adrenergic receptor, extramembrane domains, GPCR, loop dynamics, protein dynamics, protein network},
	issn = {0887-3585},
	doi = {10.1002/prot.26613},
	author = {Nikte, Siddhanta V. and Joshi, Manali and Sengupta, Durba}
}
