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Structure paper

TitleHigh-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875.
Journal, issue, pagesNature, Vol. 513, Page 124-127, Year 2014
Publish dateMay 7, 2014 (structure data deposition date)
AuthorsSrivastava, A. / Yano, J. / Hirozane, Y. / Kefala, G. / Gruswitz, F. / Snell, G. / Lane, W. / Ivetac, A. / Aertgeerts, K. / Nguyen, J. ...Srivastava, A. / Yano, J. / Hirozane, Y. / Kefala, G. / Gruswitz, F. / Snell, G. / Lane, W. / Ivetac, A. / Aertgeerts, K. / Nguyen, J. / Jennings, A. / Okada, K.
External linksNature / PubMed:25043059
MethodsX-ray diffraction
Resolution2.332 Å
Structure data

PDB-4phu:
Crystal structure of Human GPR40 bound to allosteric agonist TAK-875
Method: X-RAY DIFFRACTION / Resolution: 2.332 Å

Chemicals

ChemComp-2YB:
[(3S)-6-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy]biphenyl-3-yl}methoxy)-2,3-dihydro-1-benzofuran-3-yl]acetic acid

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • enterobacteria phage t4 (virus)
KeywordsFatty acid binding protein/Hydrolase / GPR40 / fatty acid binding protein / class A / g-protein coupled receptor / type II diabetes / TAK-875 / fasiglifam / Fatty acid binding protein-Hydrolase complex

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