2mso | pdb_00002mso

Solution study of cGm9a

spinqualitylabelsall models 2mso Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mso is a 1 chain structure with sequence from Conus gloriamaris. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CP91_CONGL Elicits "spasmodic" symptomatology. Publication Abstract from PubMed Peptide backbone cyclization is a widely used approach to improve the activity and stability of small peptides but until recently had not been applied to peptides with multiple disulfide bonds. Conotoxins are disulfide-rich conopeptides derived from the venoms of cone snails that have applications in drug design and development. However, because of their peptidic nature, they can suffer from poor bioavailability and poor stability in vivo. In this study two P-superfamily conotoxins, gm9a and bru9a, were backbone cyclised by joining the N- and C-termini with short peptide linkers using intramolecular native chemical ligation chemistry. The cyclised derivatives had conformations similar to the native peptides showing that backbone cyclization can be applied to three disulfide-bonded peptides with cystine knot motifs. Cyclic gm9a was more potent at high voltage-activated (HVA) calcium channels than its acyclic counterpart, highlighting the value of this approach in developing active and stable conotoxins containing cyclic cystine knot motifs. This article is protected by copyright. All rights reserved. Transforming conotoxins into cyclotides: Backbone cyclization of P-superfamily conotoxins.,Akcan M, Clark RJ, Daly NL, Conibear AC, de Faoite A, Heghinian MD, Sahil T, Adams DJ, Mari F, Craik DJ Biopolymers. 2015 Jul 14. doi: 10.1002/bip.22699. PMID:26172377 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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