1SBU
NMR structure of a peptide containing a dimetylthiazolidine : an analog of delta conotoxin EVIA loop 2
Summary for 1SBU
| Entry DOI | 10.2210/pdb1sbu/pdb |
| Descriptor | delta-conotoxin EVIA (1 entity in total) |
| Functional Keywords | cis leu-(dmt)thiazolidine amide bond, dimethyl-thiazolidine, vi beta turn, nmr spectroscopy, molecular dynamics simulations, toxin |
| Biological source | Conus ermineus (Atlantic fish-hunting cone) |
| Total number of polymer chains | 1 |
| Total formula weight | 1163.41 |
| Authors | Figuet, M.,Chierici, S.,Jourdan, M.,Dumy, P. (deposition date: 2004-02-11, release date: 2004-02-24, Last modification date: 2024-11-20) |
| Primary citation | Chierici, S.,Jourdan, M.,Figuet, M.,Dumy, P. A case study of 2,2-dimethylthiazolidine as locked cis proline amide bond: synthesis, NMR and molecular modeling studies of a [small delta]-conotoxin EVIA peptide analog. Org.Biomol.Chem., 2:2437-2441, 2004 Cited by PubMed Abstract: The delta-conotoxin EVIA from the Conus ermineus venom, a recently characterized toxin, exhibits cis-trans isomerism of the Leu12-Pro13 bond associated with the triggering of its biological activity. In this paper we use the pseudoproline concept to target the presumed bioactive cis conformation. We report the design and the synthesis of loop 2 analogs from residue 8 to 18 containing either the cis-inducing Cys(PsiMe,MePro)13 unit or the natural proline residue. NMR studies in water and molecular modeling allowed us to identify the amide bond "locked" in a cis conformation for as in the suggested bioactive form of the natural toxin. PubMed: 15326523DOI: 10.1039/b408325c PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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