9m87

Mo1033, Conopressin from Conus monile

spinqualitylabelsall models 9m87 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9m87 is a 1 chain structure with sequence from Conus monile. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Conopressins are single disulfide conopeptides with a close sequence similarity to vasopressin and oxytocin, exhibiting grooming and scratching effects in rodents. Here, we have investigated the impact of stereochemistry on the conserved arginine residue at position 4 and the truncation (Tr-Mo976 and Tr-Mo977) on the structure and activity of conopressins. 3D structures determined by solution NMR revealed distinct structural features for Mo1033 and (D)R4-Mo1033. Molecular dynamics studies of the conopressins with oxytocin and V2 receptor complexes revealed that both Tr-Mo976 and Tr-Mo977 showed robust interactions with the OT receptor and reduced interactions with the V2 receptor. In addition, conopressins exhibited anti-inflammatory and antioxidant potential in LPS-stimulated macrophages. Behavioural studies in mice demonstrated high grooming and scratching behaviour for Tr-Mo976 and reduced locomotory activity with Tr-Mo977. To this end, results suggest that both the truncation of the tail region and the nature of residue 8 play an essential role in altering the activity of conopressins. Structure and activity of conopressins: insights into in silico oxytocin/V2 receptor interactions, anti-inflammatory potential, and behavioural studies.,Dhurjad P, Bazaz MR, Pati S, Dandekar MP, Godugu C, Sonti R RSC Med Chem. 2025 Jul 4. doi: 10.1039/d5md00288e. PMID:40726970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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