Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains

By C. Dann, J. Hsieh, A. Rattner, D. Sharma, J. Nathans, D. Leahy. 2001

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In Molecular Biology

Citations in the corpus

ECOD: An Evolutionary Classification of Protein Domains (2014, background): “13(a)) [52], mouse SFRP3 [52], and rat MuSK [53]”
Wnt/β-catenin signaling and disease. (2012, unknown): “, 1996) that provide a primary platform for Wnt binding (Dann et al., 2001; Janda et al., 2012).”
Beyond Wnt inhibition: new functions of secreted Frizzled-related proteins in development and disease (2008, background): “SFRPs bind to, and possibly activate, Frizzled receptors The crystallographic resolution of the structure of the mouse SFRP3 and Fz8 CRD domains suggested that CRDs might be able to homodimerise or heterodimerise (Dann et al., 2001).”
INTERNATIONAL UNION OF BASIC AND CLINICAL PHARMACOLOGY REVIEW WNT/Frizzled signalling: receptor-ligand selectivity with focus on FZD-G protein signalling and its physiological relevance: IUPHAR Review 3 (2014, unknown): “Thereby, it was shown that the CRDs are ∼160 residue and primarily consist of α-helical proteins (Dann et al., 2001; Janda et al., 2012).”
The Wnt signaling pathway in development and disease. (2004, background): “Wnt proteins bind directly to the Fz CRD (Bhanot et al. 1996, Dann et al. 2001, Hsieh et al. 1999b).”
Wnts and Hedgehogs: lipid-modified proteins and similarities in signaling mechanisms at the cell surface (2003, background): “Smo is not thought to interact with an extracellular ligand, whereas Wnt proteins bind directly to the CRD of Fz (Bhanot et al., 1996; Dann et al., 2001; Hsieh et al., 1999b).”
Hedgehog signaling in animal development: paradigms and principles. (2001, background): “Smo belongs to the superfamily of G-protein-coupled receptor (GPCR) polytopic membrane-spanning proteins, being most closely related to the Frizzled family of Wnt receptors (Wodarz and Nusse 1998; Dann et al. 2001).”