NDLI: Local and global interpretations of a disease-causing mutation near the ligand entry path in hyperpolarization-activated cAMP-gated channel.

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Local and global interpretations of a disease-causing mutation near the ligand entry path in hyperpolarization-activated cAMP-gated channel.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Xu, Xinping Marni, Farzana Wu, Shengjun Su, Zhuocheng Musayev, Faik Shrestha, Sabisha Xie, Changan Gao, Weihua Liu, Qinglian Zhou, Lei
Description	Country affiliation: United States Author Affiliation: Xu X ( Department of Physiology and Biophysics, School of Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA.)
Abstract	Hyperpolarization-activated, cAMP-gated (HCN) channels sense membrane potential and intracellular cAMP levels. A mutation identified in the cAMP binding domain (CNBD) of the human HCN4 channel, S672R, severely reduces the heart rate, but the molecular mechanism has been unclear. Our biochemical binding assays on isolated CNBD and patch-clamp recordings on the functional channel show that S672R reduces cAMP binding. The crystal structure of the mutant CNBD revealed no global changes except a disordered loop on the cAMP entry path. To address this localized structural perturbation at a whole protein level, we studied the activity-dependent dynamic interaction between cAMP and the functional channel using the patch-clamp fluorometry technique. S672R reduces the binding of cAMP to the channels in the resting state and significantly increases the unbinding rate during channel deactivation. This study on a disease-causing mutation illustrates the important roles played by the structural elements on the ligand entry-exit path in stabilizing the bound ligand in the binding pocket.
File Format	HTM / HTML
ISSN	09692126
Issue Number	12
Volume Number	20
e-ISSN	18784186
Journal	Structure
Language	English
Publisher	Elsevier
Publisher Date	2012-12-05
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Cyclic Nucleotide-gated Cation Channels Genetics Muscle Proteins Mutation, Missense Amino Acid Motifs Animals Binding Sites Crystallography, X-ray Cyclic Amp Chemistry Physiology Metabolism Fluorescence Polarization Humans Hyperpolarization-activated Cyclic Nucleotide-gated Channels Kinetics Models, Molecular Patch-clamp Techniques Potassium Channels Protein Binding Protein Structure, Tertiary Xenopus Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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Local and global interpretations of a disease-causing mutation near the ligand entry path in hyperpolarization-activated cAMP-gated channel.

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