PROSITE documentation PDOC60027Contryphan family signature
Contryphans are a family of short disulfide constrained peptides isolated from various species of cone shell. They constitute a group of conopeptides that are known to contain an unusual density of post-translational modifications including tryptophan bromination, amidation of the C-terminal residue, leucine, and tryptophan isomerization, proline hydroxylation and glutamic acid γ-carboxylation [1,2,3,4,5].
Contryphans share the conserved sequence motif, CP*(D-W or D-L)XPWC, that includes a tryptophan or leucine in the D-conformation, a disulfide bond between the two cysteines, and in some cases hydroxylation of the proline preceding the D-Trp residue, Pro*. The N-terminal Cys-Pro/Hyp (hydroxyproline) peptide bond exhibits cis-trans isomerization in most contryphans; however the more abundant cis isomer is believed to be the functionally relevant conformer. The contryphan fold consists of a seven residue loop stabilized by a disulfide bridge (see <PDB:1DFY> and <PDB:1DFZ>) [1,3,5].
This family includes:
- Contryphan-P and Leu-contryphan-P from Conus purpurascens (Purple cone).
- Contryphan-Tx, contryphan-R/Tx and Leu-contryphan-Tx from Conus textile (Cloth-of-gold cone) [2].
- Glacontryphan-M from Conus marmoreus (Marble cone), a calcium-dependent inhibitor of L-type voltage-gated Ca2+ channels [4,5].
- Contryphan from Conus radiatus (Rayed cone).
- Contryphan-Sm from Conus stercusmuscarum (Fly-specked cone) [1].
- Contryphan-Vn from Conus ventricosus (Mediterranean cone) [3].
We have developed a pattern that contains the two conserved cysteines.
Expert(s) to contact by email: Last update:March 2008 / Pattern revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Pallaghy P.K. He W. Jimenez E.C. Olivera B.M. Norton R.S. |
| Title | Structures of the contryphan family of cyclic peptides. Role of electrostatic interactions in cis-trans isomerism. | |
| Source | Biochemistry 39:12845-12852(2000). | |
| PubMed ID | 11041849 |
| 2 | Authors | Jimenez E.C. Watkins M. Juszczak L.J. Cruz L.J. Olivera B.M. |
| Title | Contryphans from Conus textile venom ducts. | |
| Source | Toxicon 39:803-808(2001). | |
| PubMed ID | 11137539 |
| 3 | Authors | Eliseo T. Cicero D.O. Romeo C. Schinina M.E. Massilia G.R. Polticelli F. Ascenzi P. Paci M. |
| Title | Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator. | |
| Source | Biopolymers 74:189-198(2004). | |
| PubMed ID | 15150794 | |
| DOI | 10.1002/bip.20025 |
| 4 | Authors | Hansson K. Ma X. Eliasson L. Czerwiec E. Furie B. Furie B.C. Rorsman P. Stenflo J. |
| Title | The first gamma-carboxyglutamic acid-containing contryphan. A selective L-type calcium ion channel blocker isolated from the venom of Conus marmoreus. | |
| Source | J. Biol. Chem. 279:32453-32463(2004). | |
| PubMed ID | 15155730 | |
| DOI | 10.1074/jbc.M313825200 |
| 5 | Authors | Grant M.A. Hansson K. Furie B.C. Furie B. Stenflo J. Rigby A.C. |
| Title | The metal-free and calcium-bound structures of a gamma-carboxyglutamic acid-containing contryphan from Conus marmoreus, glacontryphan-M. | |
| Source | J. Biol. Chem. 279:32464-32473(2004). | |
| PubMed ID | 15155731 | |
| DOI | 10.1074/jbc.M313826200 |
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