Wnt is a lipid-modified morphogen and plays an important role in body development mainly through Frizzled receptors. On May 31, Science magazine published Claudia Y. Janda and other research papers online, revealing the structural biological mechanism of Frizzled recognition of Wnt.
The researchers resolved the structure of the complex of the Xenopus laevis Wnt8 (XWnt8) and mouse Frizzled-8 cysteine-rich domain (Fz8-CRD) at a resolution of 3.25 Amy. They discovered an unusual Wnt two-domain structure. This mechanism seems to be different from the known protein folding: it is like a hand, holding the Fz8-CRD at two different binding sites with the thumb and index finger. One of the sites was occupied by palmitoleate groups extending from serine 187 at the tip of the thumb structure of the Wnt molecule. At another binding site, the hydrophobic amino acid contained at the tip of the conserved Wnt index finger structure is in contact with the depression on the reverse side of the Fz8-CRD domain. The amino acid conservation at these two interfaces seems to promote the cross-reaction between the ligand and the receptor.
This research is of great significance for understanding the versatility of Wnt and designing anti-tumor and regenerative medicines accordingly.
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