| Structural highlights
1wct is a 1 chain structure with sequence from Conus textile. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Solution NMR, 1 model |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CT5AS_CONTE Epsilon-conotoxins act at presynaptic membranes, blocking the calcium channels or G protein-coupled receptors. Causes hyperactivity upon intracranial injection into mice. Causes dorsal fins drooping in fish.[1]
Publication Abstract from PubMed
Cone snails are gastropod mollusks of the genus Conus that live in tropical marine habitats. They are predators that paralyze their prey by injection of venom containing a plethora of small, conformationally constrained peptides (conotoxins). We report the identification, characterization, and structure of a gamma-carboxyglutamic acid-containing peptide, conotoxin epsilon-TxIX, isolated from the venom of the molluscivorous cone snail, Conus textile. The disulfide bonding pattern of the four cysteine residues, an unparalleled degree of posttranslational processing including bromination, hydroxylation, and glycosylation define a family of conotoxins that may target presynaptic Ca2+ channels or act on G protein-coupled presynaptic receptors via another mechanism. This conotoxin selectively reduces neurotransmitter release at an Aplysia cholinergic synapse by reducing the presynaptic influx of Ca2+ in a slow and reversible fashion. The three-dimensional structure, determined by two-dimensional 1H NMR spectroscopy, identifies an electronegative patch created by the side chains of two gamma-carboxyglutamic acid residues that extend outward from a cavernous cleft. The glycosylated threonine and hydroxylated proline enclose a localized hydrophobic region centered on the brominated tryptophan residue within the constrained intercysteine region.
A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influx.,Rigby AC, Lucas-Meunier E, Kalume DE, Czerwiec E, Hambe B, Dahlqvist I, Fossier P, Baux G, Roepstorff P, Baleja JD, Furie BC, Furie B, Stenflo J Proc Natl Acad Sci U S A. 1999 May 11;96(10):5758-63. PMID:10318957[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rigby AC, Lucas-Meunier E, Kalume DE, Czerwiec E, Hambe B, Dahlqvist I, Fossier P, Baux G, Roepstorff P, Baleja JD, Furie BC, Furie B, Stenflo J. A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influx. Proc Natl Acad Sci U S A. 1999 May 11;96(10):5758-63. PMID:10318957
- ↑ Rigby AC, Lucas-Meunier E, Kalume DE, Czerwiec E, Hambe B, Dahlqvist I, Fossier P, Baux G, Roepstorff P, Baleja JD, Furie BC, Furie B, Stenflo J. A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influx. Proc Natl Acad Sci U S A. 1999 May 11;96(10):5758-63. PMID:10318957
|
