4TTL
Racemic structure of cyclic Vc1.1 (cVc1.1-1)
Summary for 4TTL
| Entry DOI | 10.2210/pdb4ttl/pdb |
| Descriptor | Alpha-conotoxin Vc1A (2 entities in total) |
| Functional Keywords | cyclic peptide, disulfide bond, toxin |
| Biological source | Conus victoriae (Queen Victoria cone) |
| Total number of polymer chains | 1 |
| Total formula weight | 2184.37 |
| Authors | Wang, C.K.,King, G.J.,Craik, D.J. (deposition date: 2014-06-22, release date: 2014-09-10, Last modification date: 2024-11-06) |
| Primary citation | Wang, C.K.,King, G.J.,Northfield, S.E.,Ojeda, P.G.,Craik, D.J. Racemic and Quasi-Racemic X-ray Structures of Cyclic Disulfide-Rich Peptide Drug Scaffolds. Angew.Chem.Int.Ed.Engl., 53:11236-11241, 2014 Cited by PubMed Abstract: Cyclic disulfide-rich peptides have exceptional stability and are promising frameworks for drug design. We were interested in obtaining X-ray structures of these peptides to assist in drug design applications, but disulfide-rich peptides can be notoriously difficult to crystallize. To overcome this limitation, we chemically synthesized the L- and D-forms of three prototypic cyclic disulfide-rich peptides: SFTI-1 (14-mer with one disulfide bond), cVc1.1 (22-mer with two disulfide bonds), and kB1 (29-mer with three disulfide bonds) for racemic crystallization studies. Facile crystal formation occurred from a racemic mixture of each peptide, giving structures solved at resolutions from 1.25 Å to 1.9 Å. Additionally, we obtained the quasi-racemic structures of two mutants of kB1, [G6A]kB1, and [V25A]kB1, which were solved at a resolution of 1.25 Å and 2.3 Å, respectively. The racemic crystallography approach appears to have broad utility in the structural biology of cyclic peptides. PubMed: 25168664DOI: 10.1002/anie.201406563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7004 Å) |
Structure validation
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