3cmh | pdb_00003cmh

SYNTHETIC LINEAR TRUNCATED ENDOTHELIN-1 AGONIST

spinqualitylabelsall models 3cmh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cmh is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: AIB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EDN1_RAT Endothelins are endothelium-derived vasoconstrictor peptides. Publication Abstract from PubMed The solution structure of a biologically active modified linear endothelin-1 analogue, ET1-21[Cys(Acm)1,15, Aib3,11, Leu7], has been determined for the first time by two-dimensional nuclear magnetic resonance spectroscopy in a methanol-d3/water solvent mixture. Out of approximately one hundred linear peptide analogues tested by biological assay, this peptide, together with a dozen others, showed significant ETB selective agonist activity. Here we report the solution structure of an ETB selective agonist of a full-length, synthetic linear endothelin analogue. The calculated structures indicate that the peptide adopts an alpha-helical conformation between residues Ser5-His16, whilst both N- and C-termini show no preferred conformation. These results suggest that the disulphide bridges normally associated with endothelin and sarafotoxin peptides may not necessarily be important for either ETB receptor binding activity or the formation of a helical conformation in solution. Solution structure of a novel ETB receptor selective agonist ET1-21 [Cys(Acm)1,15, Aib3,11, Leu7] by nuclear magnetic resonance spectroscopy and molecular modelling.,Hewage CM, Jiang L, Parkinson JA, Ramage R, Sadler IH J Pept Res. 1999 Mar;53(3):223-33. PMID:10231710 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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