1QFB
THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS
Summary for 1QFB
| Entry DOI | 10.2210/pdb1qfb/pdb |
| NMR Information | BMRB: 4406 |
| Descriptor | PROTEIN (CONTRYPHAN-R) (1 entity in total) |
| Functional Keywords | cyclic peptide, disulfide bridge, d-configuration, conus peptide, stiff-tail syndrome, venom duct peptide, toxin |
| Total number of polymer chains | 1 |
| Total formula weight | 991.12 |
| Authors | Pallaghy, P.K.,Melnikova, A.P.,Jimenez, E.C.,Olivera, B.M.,Norton, R.S. (deposition date: 1999-04-08, release date: 1999-09-29, Last modification date: 2023-12-27) |
| Primary citation | Pallaghy, P.K.,Melnikova, A.P.,Jimenez, E.C.,Olivera, B.M.,Norton, R.S. Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops. Biochemistry, 38:11553-11559, 1999 Cited by PubMed Abstract: Contryphan-R is a disulfide-constrained octapeptide containing a D-tryptophan that was isolated recently from venom of the cone shell Conus radiatus. The polypeptide is present in two forms in solution due to cis-trans isomerization at hydroxyproline 3. The solution structure of the major form of this unusual polypeptide, determined from NMR data, consists of a well-defined fold containing a non-hydrogen-bonded chain reversal from Gly1 to Glu5, which includes a cis-hydroxyproline and a D-Trp, and a type I beta-turn from Glu5 to Cys8. The presence of a putative salt bridge between the Glu5 carboxyl group and the N-terminal ammonium group is investigated by using various solvation models during energy minimization and is compared with the results of a pH titration. A comparison of the structure of contryphan-R with other cyclic peptide structures highlights some of the key structural determinants of these peptides and suggests that the contryphan-R fold could be exploited as a scaffold onto which unrelated protein binding surfaces could be grafted. Comparison with small disulfide-bridged loops in larger proteins shows that contryphan-R is similar to a commonly occurring loop structure found in proteins. PubMed: 10471307DOI: 10.1021/bi990685j PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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