1wct
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1wct |SIZE=350|CAPTION= <scene name='initialview01'>1wct</scene> | |PDB= 1wct |SIZE=350|CAPTION= <scene name='initialview01'>1wct</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=BTR:6-BROMO-TRYPTOPHAN'>BTR</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=GTH:3-O-GLUCOPYRANOSYL-THREONINE-[2-DEOXY-2-ACETAMIDO-GLUCOPYRANOSIDE]'>GTH</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wct OCA], [http://www.ebi.ac.uk/pdbsum/1wct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wct RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: novel omega conotoxin]] | [[Category: novel omega conotoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:31 2008'' |
Revision as of 21:34, 30 March 2008
| |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A NOVEL CONOTOXIN FROM CONUS TEXTILE WITH UNUSUAL POST-TRANSLATIONAL MODIFICATIONS REDUCES PRESYNAPTIC CALCIUM INFLUX, NMR, 1 STRUCTURE, GLYCOSYLATED PROTEIN
Overview
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.
About this Structure
1WCT is a Single protein structure of sequence from Conus textile. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:34:31 2008
