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TitleAllosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation.
Journal, issue, pagesNature, Vol. 535, Page 448-452, Year 2016
Publish dateMay 5, 2016 (structure data deposition date)
AuthorsStaus, D.P. / Strachan, R.T. / Manglik, A. / Pani, B. / Kahsai, A.W. / Kim, T.H. / Wingler, L.M. / Ahn, S. / Chatterjee, A. / Masoudi, A. ...Staus, D.P. / Strachan, R.T. / Manglik, A. / Pani, B. / Kahsai, A.W. / Kim, T.H. / Wingler, L.M. / Ahn, S. / Chatterjee, A. / Masoudi, A. / Kruse, A.C. / Pardon, E. / Steyaert, J. / Weis, W.I. / Prosser, R.S. / Kobilka, B.K. / Costa, T. / Lefkowitz, R.J.
External linksNature / PubMed:27409812
MethodsX-ray diffraction
Resolution3.2 Å
Structure data

PDB-5jqh:
Structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, Nb60
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-CAU:
(2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol

ChemComp-CLR:
CHOLESTEROL

Source
  • enterobacteria phage t4 (virus)
  • homo sapiens (human)
  • lama glama (llama)
Keywordssignaling protein / hydrolase/inhibitor / GPCR / Signaling / Nanobody / Allostery / HYDROLASE / hydrolase-inhibitor complex

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