1QFB

THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS

1QFB の概要

• エントリーDOI: 10.2210/pdb1qfb/pdb
• NMR情報: BMRB: 4406
• 分子名称: PROTEIN (CONTRYPHAN-R) (1 entity in total)
• 機能のキーワード: cyclic peptide, disulfide bridge, d-configuration, conus peptide, stiff-tail syndrome, venom duct peptide, toxin
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 991.12

構造登録者

Pallaghy, P.K.,Melnikova, A.P.,Jimenez, E.C.,Olivera, B.M.,Norton, R.S. (登録日: 1999-04-08, 公開日: 1999-09-29, 最終更新日: 2023-12-27)

主引用文献

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

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: 10471307
DOI: 10.1021/bi990685j

実験手法

SOLUTION NMR