1l6o

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1l6o, resolution 2.200Å

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XENOPUS DISHEVELLED PDZ DOMAIN

Overview

Dapper was isolated in a screen for proteins interacting with Dishevelled, a key factor in Wnt signaling. Dapper and Dishevelled colocalize, intracellularly and form a complex with Axin, GSK-3, CKI, and, beta-catenin. Overexpression of Dapper increases Axin and GSK-3 in this, complex, resulting in decreased soluble beta-catenin and decreased, activation of beta-catenin-responsive genes. Dapper also inhibits, activation by Dishevelled of c-Jun N-terminal kinase (JNK), a component of, beta-catenin-independent Frizzled signaling. Inhibition of Dapper, activates both beta-catenin-responsive genes and an AP1-responsive, promoter, demonstrating that Dapper is a general Dishevelled antagonist., Depletion of maternal Dapper RNA from Xenopus embryos results in loss of, notochord and head structures, demonstrating that Dapper is required for, normal vertebrate development.

About this Structure

1L6O is a Protein complex structure of sequences from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK signaling, is required for notochord formation., Cheyette BN, Waxman JS, Miller JR, Takemaru K, Sheldahl LC, Khlebtsova N, Fox EP, Earnest T, Moon RT, Dev Cell. 2002 Apr;2(4):449-61. PMID:11970895

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