1DG2

SOLUTION CONFORMATION OF A-CONOTOXIN AUIB

1DG2 の概要

• エントリーDOI: 10.2210/pdb1dg2/pdb
• 分子名称: A-CONOTOXIN AUIB (1 entity in total)
• 機能のキーワード: a-helix, two disulfide bonds and c-term amidation, toxin
• 由来する生物種: Conus aulicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1575.79

構造登録者

Cho, J.-H.,Mok, K.H.,Olivera, B.M.,McIntosh, J.M.,Park, K.-H.,Han, K.-H. (登録日: 1999-11-23, 公開日: 2000-02-25, 最終更新日: 2024-11-06)

主引用文献

Cho, J.H.,Mok, K.H.,Olivera, B.M.,McIntosh, J.M.,Park, K.H.,Han, K.H.
Nuclear magnetic resonance solution conformation of alpha-conotoxin AuIB, an alpha(3)beta(4) subtype-selective neuronal nicotinic acetylcholine receptor antagonist.
J.Biol.Chem., 275:8680-8685, 2000

PubMed Abstract: The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of alpha and beta subunits. alpha-Conotoxins are a homologous series of small peptides that antagonize these receptors. We present the three-dimensional solution structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin known to selectively block the alpha(3)beta(4) nicotinic acetylcholine receptor subtype. The pairwise backbone and heavy-atom root mean square deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of Tyr(15), normally present in other alpha4/7 members, results in tight bending of the backbone at the C terminus and effectively renders Asp(14) to assume the spatial location of Tyr(15) present in other neuronal alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows different electrostatic surface charge distributions, which may be important in differential receptor subtype recognition.

PubMed: 10722709
DOI: 10.1074/jbc.275.12.8680

実験手法

SOLUTION NMR