02278nas a2200169   4500008004100000245009600041210006900137260000800206300001400214490000900228520167400237100001701911700001801928700002001946700002801966856011401994       2016                        eng d00aGanglioside GM1 interacts with the serotonin1A receptor via the sphingolipid binding domain0 aGanglioside GM1 interacts with the serotonin1A receptor via the   cNOV  a2818-28260 v18583 a<p>Glycosphingolipids are minor yet essential components of eukaryotic cell membranes and are involved in a variety of cellular processes. Although glycosphingolipids such as GM1 have been previously reported to influence the function of G protein-coupled receptors (GPCRs), the molecular mechanism remains elusive. In this paper, we have explored the interaction of GM1 with the serotonin1A receptor, an important neurotransmitter receptor that belongs to the GPCR family. To examine the molecular basis of the interaction of GM1 with the serotonin1A receptor, we performed a series of coarse-grain molecular dynamics simulations of the receptor embedded in membrane bilayers containing GM1. Our results show that GM1 interacts with the serotonin1A receptor predominantly at the extracellular loop 1 and specifically at the sphingolipid binding domain (SBD). The SBD motif consists of a characteristic combination of aromatic, basic and turn-inducing residues, and is evolutionarily conserved in case of the serotonin1A receptor. The interaction of the SBD site with GM1 appears to stabilize a 'flip-out' conformation in which W102 of the extracellular loop 1 flips out from the central lumen of the receptor toward the membrane. The population of the 'flip-out' conformation is increased in the presence of cholesterol. Our data strongly suggest that a direct interaction between GM1 and the SBD site of the serotonin1A receptor may occur in vivo. In view of the reported role of GM1 and the serotonin1A receptor in neurodegenerative diseases, GM1-receptor interaction assumes significance in the context of malfunctioning of neuronal GPCRs under such conditions.</p>1 aPrasanna, X.1 aJafurulla, M.1 aSengupta, Durba1 aChattopadhyay, Amitabha  uhttps://library.ncl.res.in/content/ganglioside-gm1-interacts-serotonin1a-receptor-sphingolipid-binding-domain02522nas a2200229   4500008004100000022001400041245013800055210006900193260000800262300001100270490000800281520168400289653002401973653001001997653004502007653003302052100002202085700002202107700002202129700002002151856012102171       2022                        eng d  a1047-847700aGraphical Biology Insights into the dynamic interactions at chemokine-receptor interfaces and mechanistic models of chemokine binding0 aGraphical Biology Insights into the dynamic interactions at chem  cSEP  a1078770 v2143 a<p>
	Chemokine receptors are the central signaling hubs of several processes such as cell migration, chemotaxis and cell positioning. In this graphical review, we provide an overview of the structural and mechanistic principles governing chemokine recognition that are currently emerging. Structural models of chemokine-receptor cocomplexes with endogenous chemokines, viral chemokines and therapeutics have been resolved that highlight multiple interaction sites, termed as CRS1, CRS1.5 etc. The first site of interaction has been shown to be the Nterminal domain of the receptors (CRS1 site). A large structural flexibility of the N-terminal domain has been reported that was supported by both experimental and simulation studies. Upon chemokine binding, the Nterminal domain appears to show constricted dynamics and opens up to interact with the chemokine via a large interface. The subsequent sites such as CRS1.5 and CRS2 sites have been structurally well resolved although differences arise such as the localization of the N-terminus of the ligand to a major or minor pocket of the orthosteric binding site. Several computational studies have highlighted the dynamic protein-protein interface at the CRS1 site that seemingly appears to resolve the differences in NMR and mutagenesis studies. Interestingly, the differential dynamics at the CRS1 site suggests a mixed model of binding with complex signatures of both conformational selection and induced fit models. Integrative experimental and computational approaches could help unravel the structural basis of promiscuity and specificity in chemokine-receptor binding and open up new avenues of therapeutic design.</p>
10aChemokine receptors10aGPCRs10aIntrinsically disordered protein domains10aprotein-protein interactions1 aSonawani, Archana1 aKharche, Shalmali1 aDasgupta, Debjani1 aSengupta, Durba  uhttps://library.ncl.res.in/content/graphical-biology-insights-dynamic-interactions-chemokine-receptor-interfaces-and00471nas a2200169   4500008004100000022001400041245003400055210003000089260000800119490000800127100002400135700002300159700002000182700001800202700002300220856005800243       2025                        eng d  a0032-088900aIs GCR1 the GPR157 of plants?0 aGCR1 the GPR157 of plants  cFEB0 v1971 aGotkhindikar, Aditi1 aChakravorty, David1 aSengupta, Durba1 aJoshi, Manali1 aAssmann, Sarah, M.  uhttps://library.ncl.res.in/content/gcr1-gpr157-plants