کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2493929 1115536 2011 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels
موضوعات مرتبط
علوم زیستی و بیوفناوری علم عصب شناسی علوم اعصاب رفتاری
پیش نمایش صفحه اول مقاله
3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels
چکیده انگلیسی

Pentameric ligand-gated ion channels mediate rapid chemo-electric signal transduction in animals. The active site of this family of proteins is their ion channel pore, which is located at the center of the transmembrane domain. The opening/closing motions of the channel pore are governed by the binding of neurotransmitter to the extracellular domain, but also by allosteric effectors acting within the transmembrane domain. Here, we review the structure of the transmembrane domain as well as its role in the allosteric modulation of pentameric ligand-gated ion channel function. We focus on two examples: the interactions of nicotinic ACh receptors with lipids, for which a novel “uncoupled” state has been proposed, and the interactions of GABAA and Glycine receptors with allosteric modulators, such as general anesthetics, ethanol and neurosteroids. We revisit these data in light of the recently solved X-ray structures of bacterial members of the family, which provide atomic-resolution insight into the structures of both the transmembrane domain and associated lipids.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuropharmacology - Volume 60, Issue 1, January 2011, Pages 116–125
نویسندگان
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