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Structural diversity in ligand recognition by GPCRs
cris.lastimport.scopus | 2024-02-12T20:05:18Z |
dc.abstract.en | G protein-coupled receptors (GPCRs) are activated or modulated by a very large set of divergent ligands. The GPCR superfamily of cell surface receptors plays a key role in cellular signaling in the human body, being involved in nearly all physiological and pathological processes and, therefore, GPCRs are intensively investigated as drug targets. The orthosteric binding site of GPCRs is predominantly located within the transmembrane domain (TMD) but also between the TMD and extracellular domain (ETD) or only in the ETD. Many endogenous ligands of GPCRs are peptides, and this presents a challenge to develop novel drugs by mimicking them. There are also hydrophobic ligands entering the receptor binding site from the cell membrane. Apart from orthosteric ligands, there is also a very large set of allosteric ligands or modulators that together give rise to multidimensional signaling of GPCRs, which is a huge opportunity for pharmacologic efforts to develop novel therapeutics. |
dc.affiliation | Uniwersytet Warszawski |
dc.contributor.author | Niewieczerzał, Szymon |
dc.contributor.author | Jakowiecki, Jakub |
dc.contributor.author | Filipek, Sławomir |
dc.contributor.author | Miszta, Przemysław |
dc.date.accessioned | 2024-01-23T07:40:54Z |
dc.date.available | 2024-01-23T07:40:54Z |
dc.date.issued | 2020 |
dc.description.finance | Nie dotyczy |
dc.identifier.doi | 10.1016/B978-0-12-816228-6.00003-9 |
dc.identifier.uri | https://repozytorium.uw.edu.pl//handle/item/136648 |
dc.identifier.weblink | https://api.elsevier.com/content/article/PII:B9780128162286000039?httpAccept=text/xml |
dc.language | eng |
dc.pbn.affiliation | chemical sciences |
dc.publisher.ministerial | Academic Press |
dc.relation.book | GPCRs : Structure, Function and Drug Discovery |
dc.relation.pages | 43-63 |
dc.rights | ClosedAccess |
dc.sciencecloud | nosend |
dc.subject.en | Allosteric binding |
dc.subject.en | Allosteric modulators |
dc.subject.en | GPCRs |
dc.subject.en | Hydrophobic ligands |
dc.subject.en | Ligand recognition |
dc.subject.en | Ortho-allosteric binding |
dc.subject.en | Orthosteric binding |
dc.subject.en | Peptide ligands |
dc.subject.en | Receptor signaling |
dc.title | Structural diversity in ligand recognition by GPCRs |
dc.type | MonographChapter |
dspace.entity.type | Publication |