Structural basis of Smoothened regulation by its extracellular domains

Eamon F. X. Byrne, Ria Sircar, Paul S. Miller, George Hedger, Giovanni Luchetti, Sigrid Nachtergaele, Mark D. Tully, Laurel Mydock-McGrane, Douglas F. Covey, Robert P. Rambo, Mark S. P. Sansom, Simon Newstead, Rajat Rohatgi () and Christian Siebold ()
Additional contact information
Eamon F. X. Byrne: Wellcome Trust Centre for Human Genetics, University of Oxford
Ria Sircar: Stanford University School of Medicine
Paul S. Miller: Wellcome Trust Centre for Human Genetics, University of Oxford
George Hedger: University of Oxford
Giovanni Luchetti: Stanford University School of Medicine
Sigrid Nachtergaele: Stanford University School of Medicine
Mark D. Tully: Diamond Light Source Ltd, Harwell Science & Innovation Campus
Laurel Mydock-McGrane: Washington University School of Medicine
Douglas F. Covey: Washington University School of Medicine
Robert P. Rambo: Diamond Light Source Ltd, Harwell Science & Innovation Campus
Mark S. P. Sansom: University of Oxford
Simon Newstead: University of Oxford
Rajat Rohatgi: Stanford University School of Medicine
Christian Siebold: Wellcome Trust Centre for Human Genetics, University of Oxford

Nature, 2016, vol. 535, issue 7613, 517-522

Abstract: Structural studies show that the activity of the G-protein-coupled receptor Smoothened is modulated by ligand-regulated interactions between its extracellular and transmembrane domains.

Date: 2016
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DOI: 10.1038/nature18934

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