NMR spatial structure of α-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors

FEBS Letters

Volumn 444, Issue 2-3, 1999, Pages 275-280

  Maslennikov, Innokenty V ^a   Shenkarev, Zakhar O ^a   Zhmak, Maxim N ^a   Ivanov, Vadim T ^a   Methfessel, Christoph ^b   Tsetlin, Victor I ^a   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b BAYER AG   (Germany)

Author keywords

Acetylcholine receptor; Conotoxin; Neurotoxin; Nuclear magnetic resonance structure

Indexed keywords

ACETYLCHOLINE; CONOTOXIN; NEUROTOXIN; NICOTINIC RECEPTOR; SNAIL VENOM; SNAKE VENOM;

ARTICLE; BINDING SITE; CONTROLLED STUDY; NERVE CELL; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RECEPTOR BINDING; SNAIL; SNAKE;

AMINO ACID SEQUENCE; COBRA NEUROTOXINS; CONOTOXINS; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLLUSK VENOMS; NERVE TISSUE PROTEINS; NEUROTOXINS; OLIGOPEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, NICOTINIC; SNAKE VENOMS;

CONUS IMPERIALIS; GASTROPODA; SERPENTES;

EID: 0033067115     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00069-1     Document Type: Article

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