Journal article icon

Journal article

Structural basis for Smoothened regulation by its extracellular domains

Abstract:

Developmental signals of the Hedgehog (Hh) and Wnt families are transduced across the membrane by Frizzled-class G-protein coupled receptors (GPCRs) composed of both a heptahelical transmembrane domain (TMD) and an extracellular cysteine-rich domain (CRD). How such large extracellular domains of GPCRs regulate signalling by the TMD is unknown. We present crystal structures of the Hh signal transducer and oncoprotein Smoothened (SMO), which contains two distinct ligand-binding sites in its TMD...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Files:
Publisher copy:
10.1038/nature18934

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Expand authors...
Expand funders...
Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Journal website
Volume:
535
Pages:
517–522
Publication date:
2016-06-01
Acceptance date:
2016-07-20
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Source identifiers:
629467
Pubs id:
pubs:629467
UUID:
uuid:df1887bb-aba9-41da-af6b-e8b4c6bd79a3
Local pid:
pubs:629467
Deposit date:
2016-06-23

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP