1V6R
Solution Structure of Endothelin-1 with its C-terminal Folding
Summary for 1V6R
| Entry DOI | 10.2210/pdb1v6r/pdb |
| NMR Information | BMRB: 6070 |
| Descriptor | Endothelin-1 (1 entity in total) |
| Functional Keywords | endothelin, a-helix, c-terminal folding, cardiovascular bioactive peptide, g-protein coupled-receptor ligand, contractile protein |
| Cellular location | Secreted: P05305 |
| Total number of polymer chains | 1 |
| Total formula weight | 2497.95 |
| Authors | Takashima, H.,Mimura, N.,Ohkubo, T.,Yoshida, T.,Tamaoki, H.,Kobayashi, Y. (deposition date: 2003-12-03, release date: 2004-03-16, Last modification date: 2024-10-30) |
| Primary citation | Takashima, H.,Mimura, N.,Ohkubo, T.,Yoshida, T.,Tamaoki, H.,Kobayashi, Y. Distributed Computing and NMR Constraint-Based High-Resolution Structure Determination: Applied for Bioactive Peptide Endothelin-1 To Determine C-Terminal Folding J.Am.Chem.Soc., 126:4504-4505, 2004 Cited by PubMed Abstract: 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. PubMed: 15070353DOI: 10.1021/ja031637w PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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