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Structure paper

TitleFull-length human GLP-1 receptor structure without orthosteric ligands.
Journal, issue, pagesNat Commun, Vol. 11, Page 1272-1272, Year 2020
Publish dateDec 28, 2019 (structure data deposition date)
AuthorsWu, F. / Yang, L. / Hang, K. / Laursen, M. / Wu, L. / Han, G.W. / Ren, Q. / Roed, N.K. / Lin, G. / Hanson, M.A. ...Wu, F. / Yang, L. / Hang, K. / Laursen, M. / Wu, L. / Han, G.W. / Ren, Q. / Roed, N.K. / Lin, G. / Hanson, M.A. / Jiang, H. / Wang, M.W. / Reedtz-Runge, S. / Song, G. / Stevens, R.C.
External linksNat Commun / PubMed:32152292
MethodsX-ray diffraction
Resolution3.2 Å
Structure data

PDB-6ln2:
Crystal structure of full length human GLP1 receptor in complex with Fab fragment (Fab7F38)
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-97Y:
N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine

Source
  • homo sapiens (human)
  • clostridium pasteurianum (bacteria)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Full length Human GLP1 receptor / Class B / Fab7F38 / TMD / NAM PF06372222 / LCP

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