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1WCT

A NOVEL CONOTOXIN FROM CONUS TEXTILE WITH UNUSUAL POST-TRANSLATIONAL MODIFICATIONS REDUCES PRESYNAPTIC CALCIUM INFLUX, NMR, 1 STRUCTURE, GLYCOSYLATED PROTEIN

1WCT の概要
エントリーDOI10.2210/pdb1wct/pdb
分子名称OMEGAC-TXIX, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose (2 entities in total)
機能のキーワードgamma-carboxy glutamic acid, novel omega conotoxin, calcium channel blocker
由来する生物種Conus textile (cloth-of-gold cone)
細胞内の位置Secreted: P81755
タンパク質・核酸の鎖数1
化学式量合計1953.80
構造登録者
Rigby, A.C.,Hambe, B.,Czerwiec, E.,Baleja, J.D.,Furie, B.C.,Furie, B.,Stenflo, J. (登録日: 1998-12-18, 公開日: 1999-06-08, 最終更新日: 2025-03-26)
主引用文献Rigby, A.C.,Lucas-Meunier, E.,Kalume, D.E.,Czerwiec, E.,Hambe, B.,Dahlqvist, I.,Fossier, P.,Baux, G.,Roepstorff, P.,Baleja, J.D.,Furie, B.C.,Furie, B.,Stenflo, J.
A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influx.
Proc.Natl.Acad.Sci.USA, 96:5758-5763, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10318957
DOI: 10.1073/pnas.96.10.5758
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1wct
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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