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Structure and ligand recognition of class C GPCRs

The G-protein-coupled receptors (GPCRs) are one of the largest super families of cell-surface receptors and play crucial roles in virtu- ally every organ system. One particular family of GPCRs, the class C GPCRs, is distinguished by a characteristically large extracellular domain and constitutive di... Full description

Journal Title: Acta pharmacologica Sinica 2012, Vol.33 (3), p.312-323
Main Author: Chun, Lei
Other Authors: Zhang, Wen-hua , Liu, Jian-feng
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: United States: Nature Publishing Group
ID: ISSN: 1671-4083
Link: https://www.ncbi.nlm.nih.gov/pubmed/22286915
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title: Structure and ligand recognition of class C GPCRs
format: Article
creator:
  • Chun, Lei
  • Zhang, Wen-hua
  • Liu, Jian-feng
subjects:
  • allosteric modulators
  • Allosteric Site
  • allosteric sites
  • Animals
  • G-protein-coupled receptors (GPCRs)
  • G-蛋白偶联受体
  • Humans
  • Ligands
  • orthosteric sites
  • Protein Structure, Tertiary
  • Receptors, G-Protein-Coupled - chemistry
  • Receptors, G-Protein-Coupled - metabolism
  • Review
  • structure
  • 器官系统
  • 家庭成员
  • 激活机制
  • 细胞表面受体
ispartof: Acta pharmacologica Sinica, 2012, Vol.33 (3), p.312-323
description: The G-protein-coupled receptors (GPCRs) are one of the largest super families of cell-surface receptors and play crucial roles in virtu- ally every organ system. One particular family of GPCRs, the class C GPCRs, is distinguished by a characteristically large extracellular domain and constitutive dimerization. The structure and activation mechanism of this family result in potentially unique ligand recogn tion sites, thereby offering a variety of possibilities by which receptor activity might be modulated using novel compounds. In the pres- ent article, we aim to provide an overview of the exact sites and structural features involved in ligand recognition of the class C GPCRs Furthermore, we demonstrate the precise steps that occur during the receptor activation process, which underlie the possibilities by which receptor function may be altered by different approaches. Finally, we use four typical family members to illustrate orthosteric and allosteric sites with representative ligands and their corresponding therapeutic potential.
language: eng
source:
identifier: ISSN: 1671-4083
fulltext: no_fulltext
issn:
  • 1671-4083
  • 1745-7254
url: Link


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descriptionThe G-protein-coupled receptors (GPCRs) are one of the largest super families of cell-surface receptors and play crucial roles in virtu- ally every organ system. One particular family of GPCRs, the class C GPCRs, is distinguished by a characteristically large extracellular domain and constitutive dimerization. The structure and activation mechanism of this family result in potentially unique ligand recogn tion sites, thereby offering a variety of possibilities by which receptor activity might be modulated using novel compounds. In the pres- ent article, we aim to provide an overview of the exact sites and structural features involved in ligand recognition of the class C GPCRs Furthermore, we demonstrate the precise steps that occur during the receptor activation process, which underlie the possibilities by which receptor function may be altered by different approaches. Finally, we use four typical family members to illustrate orthosteric and allosteric sites with representative ligands and their corresponding therapeutic potential.
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subjectallosteric modulators ; Allosteric Site ; allosteric sites ; Animals ; G-protein-coupled receptors (GPCRs) ; G-蛋白偶联受体 ; Humans ; Ligands ; orthosteric sites ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled - chemistry ; Receptors, G-Protein-Coupled - metabolism ; Review ; structure ; 器官系统 ; 家庭成员 ; 激活机制 ; 细胞表面受体
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1The G-protein-coupled receptors (GPCRs) are one of the largest super families of cell-surface receptors and play crucial roles in virtu- ally every organ system. One particular family of GPCRs, the class C GPCRs, is distinguished by a characteristically large extracellular domain and constitutive dimerization. The structure and activation mechanism of this family result in potentially unique ligand recogn tion sites, thereby offering a variety of possibilities by which receptor activity might be modulated using novel compounds. In the pres- ent article, we aim to provide an overview of the exact sites and structural features involved in ligand recognition of the class C GPCRs Furthermore, we demonstrate the precise steps that occur during the receptor activation process, which underlie the possibilities by which receptor function may be altered by different approaches. Finally, we use four typical family members to illustrate orthosteric and allosteric sites with representative ligands and their corresponding therapeutic potential.
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abstractThe G-protein-coupled receptors (GPCRs) are one of the largest super families of cell-surface receptors and play crucial roles in virtu- ally every organ system. One particular family of GPCRs, the class C GPCRs, is distinguished by a characteristically large extracellular domain and constitutive dimerization. The structure and activation mechanism of this family result in potentially unique ligand recogn tion sites, thereby offering a variety of possibilities by which receptor activity might be modulated using novel compounds. In the pres- ent article, we aim to provide an overview of the exact sites and structural features involved in ligand recognition of the class C GPCRs Furthermore, we demonstrate the precise steps that occur during the receptor activation process, which underlie the possibilities by which receptor function may be altered by different approaches. Finally, we use four typical family members to illustrate orthosteric and allosteric sites with representative ligands and their corresponding therapeutic potential.
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