Mechanism of ?2AR regulation by an intracellular positive allosteric modulator [electronic resource]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 574.8 [Unassigned]

Thông tin xuất bản: Bethesda, Md. : Oak Ridge, Tenn. : National Institutes of Health (U.S.) ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2019

Mô tả vật lý: Size: p. 1283-1287 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 260001

 Drugs targeting the orthosteric, primary binding site of G protein?coupled receptors are the most common therapeutics. Allosteric binding sites, elsewhere on the receptors, are less well-defined, and so less exploited clinically. In this paper we report the crystal structure of the prototypic ?<
 sub>
 2<
 /sub>
 -adrenergic receptor in complex with an orthosteric agonist and compound-6FA, a positive allosteric modulator of this receptor. It binds on the receptor?s inner surface in a pocket created by intracellular loop 2 and transmembrane segments 3 and 4, stabilizing the loop in an ?-helical conformation required to engage the G protein. Structural comparison explains the selectivity of the compound for ?<
 sub>
 2<
 /sub>
 - over the ?<
 sub>
 1<
 /sub>
 -adrenergic receptor. Diversity in location, mechanism, and selectivity of allosteric ligands provides potential to expand the range of receptor drugs.
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