ArticleActa pharmacologica Sinica2024
Structural insights into somatostatin receptor 5 bound with cyclic peptides.
Article in Acta pharmacologica Sinica, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Development of dual SSTRSC medicinal chemistry · 2026Article
- Revisiting Alzheimer's Disease Through the Somatostatin-Mitochondria Axis.Molecular neurobiology · 2026Review
- Advances in Cyclic Peptides Targeting G Protein-Coupled Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Structural and dynamic insights into ligand recognition and activation of somatostatin receptor 3.Acta pharmacologica Sinica · 2026Article
- Targeting lineage-specific heterogeneity and hypovascular-fibrotic barriers may enable precision immunotherapy in pituitary neuroendocrine tumors.Frontiers in immunology · 2026Review
- Structural insights into nonpeptide antagonist inhibition of somatostatin receptor subtype 5.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
7 authors.
Funding
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Abstract
Somatostatin receptor 5 (SSTR5) is highly expressed in ACTH-secreting pituitary adenomas and is an important drug target for the treatment of Cushing's disease. Two cyclic SST analog peptides (pasireotide and octreotide) both can activate SSTR5 and SSTR2. Pasireotide is preferential binding to SSTR5 than octreotide, while octreotide is biased to SSTR2 than SSTR5. The lack of selectivity of both pasireotide and octreotide causes side effects, such as hyperglycemia, gastrointestinal disturbance, and abnormal glucose homeostasis. However, little is known about the binding and selectivity mechanisms of pasireotide and octreotide with SSTR5, limiting the development of subtype-selective SST analog drugs specifically targeting SSTR5. Here, we report two cryo-electron microscopy (cryo-EM) structures of SSTR5-Gi complexes activated by pasireotide and octreoitde at resolutions of 3.09 Å and 3.24 Å, respectively. In combination with structural analysis and functional experiments, our results reveal the molecular mechanisms of ligand recognition and receptor activation. We also demonstrate that pasireotide preferentially binds to SSTR5 through the interactions between Tyr(Bzl)/
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