原创力文档crystal structure of lymnaea stagnalis achbp complexed with the potent nachr antagonist dhβe suggests a unique mode of antagonism晶体结构的椎实螺属stagnalis achbp包裹着的乙酰拮抗剂dhβe表明一个独特的对抗方式.pdfVIP
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crystal structure of lymnaea stagnalis achbp complexed with the potent nachr antagonist dhβe suggests a unique mode of antagonism晶体结构的椎实螺属stagnalis achbp包裹着的乙酰拮抗剂dhβe表明一个独特的对抗方式
Crystal Structure of Lymnaea stagnalis AChBP
Complexed with the Potent nAChR Antagonist DH
b E
Suggests a Unique Mode of Antagonism
1 1 2 1 1
Azadeh Shahsavar , Jette S. Kastrup , Elsebet Ø. Nielsen , Jesper L. Kristensen , Michael Gajhede ,
Thomas Balle1*¤
1 Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark, 2 NeuroSearch A/S, Ballerup,
Denmark
Abstract
Nicotinic acetylcholine receptors (nAChRs) are pentameric ligand-gated ion channels that belong to the Cys-loop receptor
superfamily. These receptors are allosteric proteins that exist in different conformational states, including resting (closed),
activated (open), and desensitized (closed) states. The acetylcholine binding protein (AChBP) is a structural homologue of
the extracellular ligand-binding domain of nAChRs. In previous studies, the degree of the C-loop radial extension of AChBP
has been assigned to different conformational states of nAChRs. It has been suggested that a closed C-loop is preferred for
the active conformation of nAChRs in complex with agonists whereas an open C-loop reflects an antagonist-bound (closed)
state. In this work, we have determined the crystal structure of AChBP from the water snail Lymnaea stagnalis (Ls) in
complex with dihydro-b-erythroidine (DHbE), which is a potent competitive antagonist of nAChRs. The structure reveals that
binding of DHbE to AChBP imposes closure of the C-loop as agonists, but also a shift perpendicula
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