Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 3389, Year 2025
Publish date	Apr 10, 2025
Authors	Jianjun Cao / Matthew J Belousoff / Rachel M Johnson / Peter Keov / Zamara Mariam / Giuseppe Deganutti / George Christopoulos / Caroline A Hick / Steffen Reedtz-Runge / Tine Glendorf / Borja Ballarín-González / Kirsten Raun / Charles Bayly-Jones / Denise Wootten / Patrick M Sexton /
PubMed Abstract	Obesity is a major and increasingly prevalent chronic metabolic disease with numerous comorbidities. While recent incretin-based therapies have provided pharmaceutical inroads into treatment of ...Obesity is a major and increasingly prevalent chronic metabolic disease with numerous comorbidities. While recent incretin-based therapies have provided pharmaceutical inroads into treatment of obesity, there remains an ongoing need for additional medicines with distinct modes of action as independent or complementary therapeutics. Among the most promising candidates, supported by phase 1 and 2 clinical trials, is cagrilintide, a long-acting amylin and calcitonin receptor agonist. As such, understanding how cagrilintide functionally engages target receptors is critical for future development of this target class. Here, we determine structures of cagrilintide bound to Gs-coupled, active, amylin receptors (AMYR, AMYR, AMYR) and calcitonin receptor (CTR) and compare cagrilintide interactions and the dynamics of receptor complexes with previously reported structures of receptors bound to rat amylin, salmon calcitonin or recently developed amylin-based peptides. These data reveal that cagrilintide has an amylin-like binding mode but, compared to other peptides, induces distinct conformational dynamics at calcitonin-family receptors that could contribute to its clinical efficacy.
External links	Nat Commun / PubMed:40204768 / PubMed Central
Methods	EM (single particle)
Resolution	2.2 - 3.6 Å
Structure data	44652 9blb EMDB-44652, PDB-9blb: Human Calcitonin Receptor in Complex with Gs and Cagrilintide Backbone (non-acylated) in bypass conformation Method: EM (single particle) / Resolution: 3.2 Å 44653 9blc EMDB-44653, PDB-9blc: Human Calcitonin Receptor in Complex with Gs and Cagrilintide Backbone (non-acylated) in CT-like conformation Method: EM (single particle) / Resolution: 3.3 Å 44678 9blw EMDB-44678, PDB-9blw: Human amylin1 Receptor in complex with Gs and Cagrilintide backbone (non-acylated) Method: EM (single particle) / Resolution: 3.2 Å 44760 9bp3 EMDB-44760, PDB-9bp3: Human Amylin1 Receptor in complex with Gs and cagrilintide Method: EM (single particle) / Resolution: 2.2 Å 44796 9bq3 EMDB-44796, PDB-9bq3: Human Amylin2 Receptor in Complex with Gs and Cagrilintide Method: EM (single particle) / Resolution: 2.8 Å 44898 9btw EMDB-44898, PDB-9btw: Human Amylin3 Receptor in complex with Gs and cagrilintide Method: EM (single particle) / Resolution: 3.0 Å 44904 9bub EMDB-44904, PDB-9bub: Human calcitonin Receptor in complex with Gs and cagrilintide in the bypass conformation Method: EM (single particle) / Resolution: 2.3 Å 44905 9buc EMDB-44905, PDB-9buc: Human calcitonin Receptor in complex with Gs and cagrilintide in the bypass conformation (repeat) Method: EM (single particle) / Resolution: 3.4 Å 44906 9bud EMDB-44906, PDB-9bud: Human calcitonin Receptor in complex with Gs and cagrilintide in the CT-like conformation Method: EM (single particle) / Resolution: 2.5 Å 44907 9bue EMDB-44907, PDB-9bue: Human calcitonin Receptor in complex with Gs and cagrilintide in the CT-like conformation (repeat) Method: EM (single particle) / Resolution: 3.6 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose PDB-1b90: BACILLUS CEREUS BETA-AMYLASE APO FORM ChemComp-P42: (2S)-2-{[(1R)-1-hydroxyhexadecyl]oxy}-3-{[(1R)-1-hydroxyoctadecyl]oxy}propyl 2-(trimethylammonio)ethyl phosphate / SPPC, phospholipidYM ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-HOH*: WATER
Source	homo sapiens (human) lama glama (llama)
Keywords	MEMBRANE PROTEIN / Amylin receptor / GPCR / RAMPs / Calcitonin receptor / Cagrilintide / obesity / receptor activity-modifying protein / RAMP2