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TitlePlasticity in ligand recognition at somatostatin receptors.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 3, Page 210-217, Year 2022
Publish dateFeb 24, 2022
AuthorsMichael J Robertson / Justin G Meyerowitz / Ouliana Panova / Kenneth Borrelli / Georgios Skiniotis /
PubMed AbstractSomatostatin is a signaling peptide that plays a pivotal role in physiologic processes relating to metabolism and growth through its actions at somatostatin receptors (SSTRs). Members of the SSTR ...Somatostatin is a signaling peptide that plays a pivotal role in physiologic processes relating to metabolism and growth through its actions at somatostatin receptors (SSTRs). Members of the SSTR subfamily, particularly SSTR2, are key drug targets for neuroendocrine neoplasms, with synthetic peptide agonists currently in clinical use. Here, we show the cryogenic-electron microscopy structures of active-state SSTR2 in complex with heterotrimeric G and either the endogenous ligand SST14 or the FDA-approved drug octreotide. Complemented by biochemical assays and molecular dynamics simulations, these structures reveal key details of ligand recognition and receptor activation at SSTRs. We find that SSTR ligand recognition is highly diverse, as demonstrated by ligand-induced conformational changes in ECL2 and substantial sequence divergence across subtypes in extracellular regions. Despite this complexity, we rationalize several known sources of SSTR subtype selectivity and identify an additional interaction for specific binding. These results provide valuable insights for structure-based drug discovery at SSTRs.
External linksNat Struct Mol Biol / PubMed:35210615 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 2.7 Å
Structure data

25586

7t10

EMDB-25586, PDB-7t10:
CryoEM structure of somatostatin receptor 2 in complex with somatostatin-14 and Gi3
Method: EM (single particle) / Resolution: 2.5 Å

25587

7t11

EMDB-25587, PDB-7t11:
CryoEM structure of somatostatin receptor 2 in complex with Octreotide and Gi3.
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN/SIGNALING PROTEIN / GPCR / Receptor / Complex / MEMBRANE PROTEIN / MEMBRANE PROTEIN-SIGNALING PROTEIN complex

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