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PROSITE documentation PDOC60027

Contryphan family signature





Description

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:

Ramakumar S.

Last update:

March 2008 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

CONTRYPHAN, PS60027; Contryphan family signature  (PATTERN)


References

1AuthorsPallaghy P.K., He W., Jimenez E.C., Olivera B.M., Norton R.S.
TitleStructures of the contryphan family of cyclic peptides. Role of electrostatic interactions in cis-trans isomerism.
SourceBiochemistry 39:12845-12852(2000).
PubMed ID11041849

2AuthorsJimenez E.C., Watkins M., Juszczak L.J., Cruz L.J., Olivera B.M.
TitleContryphans from Conus textile venom ducts.
SourceToxicon 39:803-808(2001).
PubMed ID11137539

3AuthorsEliseo T., Cicero D.O., Romeo C., Schinina M.E., Massilia G.R., Polticelli F., Ascenzi P., Paci M.
TitleSolution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator.
SourceBiopolymers 74:189-198(2004).
PubMed ID15150794
DOI10.1002/bip.20025

4AuthorsHansson K., Ma X., Eliasson L., Czerwiec E., Furie B., Furie B.C., Rorsman P., Stenflo J.
TitleThe first gamma-carboxyglutamic acid-containing contryphan. A selective L-type calcium ion channel blocker isolated from the venom of Conus marmoreus.
SourceJ. Biol. Chem. 279:32453-32463(2004).
PubMed ID15155730
DOI10.1074/jbc.M313825200

5AuthorsGrant M.A., Hansson K., Furie B.C., Furie B., Stenflo J., Rigby A.C.
TitleThe metal-free and calcium-bound structures of a gamma-carboxyglutamic acid-containing contryphan from Conus marmoreus, glacontryphan-M.
SourceJ. Biol. Chem. 279:32464-32473(2004).
PubMed ID15155731
DOI10.1074/jbc.M313826200



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