【摘 要】
：
Dear Editor,rnThe ten mammalian Frizzleds (FZD1-10) belong to the class F of G protein-coupled receptors (GPCRs) and mediate WNT signaling through interaction with transducer proteins including Dishev-elled (DVL) or heterotrimeric G proteins.1 Their invol
【机 构】
：
iHuman Institute,ShanghaiTech University,Shanghai,China;School of Life Science and Technology,Shangh
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Dear Editor,rnThe ten mammalian Frizzleds (FZD1-10) belong to the class F of G protein-coupled receptors (GPCRs) and mediate WNT signaling through interaction with transducer proteins including Dishev-elled (DVL) or heterotrimeric G proteins.1 Their involvement in human disease has put FZDs at the forefront of drug targets,especially anti-cancer therapy.2 However,no drugs have been developed for efficient pharmacological modulation of FZDs,partially owing to the limited understanding of FZD structure and activation mechanisms.1,3 Among class F,FZD7 is intensively pursued due to its relevance in various tumor models,particularly in intestinal cancers.4 Detailed structures of the receptor complexes would allow for structure-guided discovery of new drug candidates.FZD1-10 share structural similarity with the related class F member Smoothened (SMO),which mediates Hedgehog signaling and is a validated target for cancer therapy.2 In an effort to understand the structural basis of FZD activation and transducer interaction,we solved the structure of human FZD7 in complex with heterotrimeric mini Gs (mGs).
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