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Structural basis for molecular recognition at serotonin receptors

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
  • Wacker, Daniel, Ph.D. in Biology, Scripps Research 2009 - 2013

authors

  • Wang, Chong
  • Jiang, Y.
  • Ma, J.
  • Wu, Huixian
  • Wacker, Daniel
  • Katritch, Vsevolod
  • Han, G. W.
  • Liu, W.
  • Huang, X. P.
  • Vardy, E.
  • McCorvy, J. D.
  • Gao, X.
  • Zhou, X. E.
  • Melcher, K.
  • Zhang, C.
  • Bai, F.
  • Yang, H.
  • Yang, L.
  • Jiang, H.
  • Roth, B. L.
  • Cherezov, Vadim
  • Stevens, Raymond
  • Xu, H. E.

publication date

  • May 2013

journal

  • Science  Journal

abstract

  • Serotonin or 5-hydroxytryptamine (5-HT) regulates a wide spectrum of human physiology through the 5-HT receptor family. We report the crystal structures of the human 5-HT1B G protein-coupled receptor bound to the agonist antimigraine medications ergotamine and dihydroergotamine. The structures reveal similar binding modes for these ligands, which occupy the orthosteric pocket and an extended binding pocket close to the extracellular loops. The orthosteric pocket is formed by residues conserved in the 5-HT receptor family, clarifying the family-wide agonist activity of 5-HT. Compared with the structure of the 5-HT2B receptor, the 5-HT1B receptor displays a 3 angstrom outward shift at the extracellular end of helix V, resulting in a more open extended pocket that explains subtype selectivity. Together with docking and mutagenesis studies, these structures provide a comprehensive structural basis for understanding receptor-ligand interactions and designing subtype-selective serotonergic drugs.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Dihydroergotamine
  • Ergotamine
  • Humans
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Ligands
  • Lysergic Acid Diethylamide
  • Models, Molecular
  • Molecular Docking Simulation
  • Molecular Sequence Data
  • Mutagenesis
  • Norfenfluramine
  • Pindolol
  • Propranolol
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Receptor, Serotonin, 5-HT1B
  • Serotonin 5-HT1 Receptor Agonists
  • Tryptamines
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Identity

PubMed Central ID

  • PMC3644373

International Standard Serial Number (ISSN)

  • 1095-9203 (Electronic) 0036-8075 (Linking)

Digital Object Identifier (DOI)

  • 10.1126/science.1232807

PubMed ID

  • 23519210
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Additional Document Info

start page

  • 610

end page

  • 614

volume

  • 340

issue

  • 6132

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