1v6r | pdb_00001v6r

Solution Structure of Endothelin-1 with its C-terminal Folding

spinqualitylabelsall models 1v6r, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v6r is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides. Publication Abstract from PubMed Distributed computing has been implemented to the solution structure determination of endothelin-1 to evaluate efficiency of the method for NMR constraint-based structure calculations. A key target of the investigation was determination of the C-terminal folding of the peptide, which had been dispersed in previous studies of NMR, despite its pharmacological significances. With use of tens of thousands of random initial structures to explore the conformational space comprehensively, we determined high-resolution structures with good convergences of C-terminal as well as previously defined N-terminal structures. The previous studies had missed the C-terminal convergence because of initial structure dependencies trapped in localized folding of the N-terminal region, which are strongly constricted by two disulfide bonds. Distributed computing and NMR constraint-based high-resolution structure determination: applied for bioactive Peptide endothelin-1 to determine C-terminal folding.,Takashima H, Mimura N, Ohkubo T, Yoshida T, Tamaoki H, Kobayashi Y J Am Chem Soc. 2004 Apr 14;126(14):4504-5. PMID:15070353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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