Visualization of the Afamin/Wnt3a complex in motion —Revealing the key role of the hydrophobic pocket—
Peer-Reviewed Publication
Updates every hour. Last Updated: 14-Jun-2026 18:16 ET (14-Jun-2026 22:16 GMT/UTC)
A joint research group consisting of Hikaru Ichida, a doctoral student in the Division of Nano Life Science, Graduate School of Frontier Science Initiative, Kanazawa University; Kosuke Mizuno, currently a Postdoctoral Researcher at the Institute for Protein Research, The University of Osaka; Professor Noriyuki Kodera and Associate Professor Holger Flechsig of the Nano Life Science Institute (WPI-NanoLSI), Kanazawa University; and Associate Professor Satoshi Toda of the Institute for Protein Research, The University of Osaka, has succeeded in visualizing the structural dynamics underlying how the serum protein Afamin stabilizes and transports Wnt3a, a lipid-modified signaling molecule. The study also showed that stable binding between these two molecules depends on both a hydrophobic pocket that accommodates Wnt3a and the structural integrity of Afamin. Wnt proteins are essential molecules that help the body develop properly and maintain healthy tissues. However, because they do not dissolve well in water and are highly hydrophobic, they tend to be unstable in the body. This study has revealed part of the mechanism by which Wnt3a is stably transported with the help of another protein. These findings are expected to deepen our understanding of biological processes involving Wnt3a and may contribute in the future to the development of ex vivo tissue engineering technologies and regenerative medicine.
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