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Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator

Academic Article
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Overview

related to degree

  • Wang, Chong, Ph.D. in Chemistry, Scripps Research , transferred from UCSD 2011 - 2014
  • Wu, Huixian, Ph.D. in Chemistry, Scripps Research 2010 - 2014

authors

  • Wu, Huixian
  • Wang, Chong
  • Gregory, K. J.
  • Han, G. W.
  • Cho, H. P.
  • Xia, Y.
  • Niswender, C. M.
  • Katritch, Vsevolod
  • Meiler, J.
  • Cherezov, Vadim
  • Conn, P. J.
  • Stevens, Raymond

publication date

  • April 2014

journal

  • Science  Journal

abstract

  • The excitatory neurotransmitter glutamate induces modulatory actions via the metabotropic glutamate receptors (mGlus), which are class C G protein-coupled receptors (GPCRs). We determined the structure of the human mGlu1 receptor seven-transmembrane (7TM) domain bound to a negative allosteric modulator, FITM, at a resolution of 2.8 angstroms. The modulator binding site partially overlaps with the orthosteric binding sites of class A GPCRs but is more restricted than most other GPCRs. We observed a parallel 7TM dimer mediated by cholesterols, which suggests that signaling initiated by glutamate's interaction with the extracellular domain might be mediated via 7TM interactions within the full-length receptor dimer. A combination of crystallography, structure-activity relationships, mutagenesis, and full-length dimer modeling provides insights about the allosteric modulation and activation mechanism of class C GPCRs.

subject areas

  • Allosteric Regulation
  • Allosteric Site
  • Amino Acid Sequence
  • Benzamides
  • Binding Sites
  • Cholesterol
  • Crystallography, X-Ray
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Conformation
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Receptors, Metabotropic Glutamate
  • Structure-Activity Relationship
  • Thiazoles
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Identity

PubMed Central ID

  • PMC3991565

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1249489

PubMed ID

  • 24603153
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Additional Document Info

start page

  • 58

end page

  • 64

volume

  • 344

issue

  • 6179

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