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1v6r
From Proteopedia
Solution Structure of Endothelin-1 with its C-terminal Folding
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.
About this Structure
1V6R is a Single protein structure. Full experimental information is available from OCA.
Reference
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
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