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1L6O

XENOPUS DISHEVELLED PDZ DOMAIN

Summary for 1L6O
Entry DOI10.2210/pdb1l6o/pdb
DescriptorSegment polarity protein dishevelled homolog DVL-2, Dapper 1 (3 entities in total)
Functional Keywordsdishevelled, wnt pathway, pdz, molecular recognition, gene regulation
Biological sourceXenopus laevis (African clawed frog)
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Cellular locationCytoplasm: P51142
Total number of polymer chains6
Total formula weight34444.42
Authors
Cheyette, B.N.R.,Waxman, J.S.,Miller, J.R.,Takemaru, K.-I.,Sheldahl, L.C.,Khlebtsova, N.,Fox, E.P.,Earnest, T.,Moon, R.T. (deposition date: 2002-03-11, release date: 2003-06-03, Last modification date: 2024-10-30)
Primary citationCheyette, B.N.R.,Waxman, J.S.,Miller, J.R.,Takemaru, K.-I.,Sheldahl, L.C.,Khlebtsova, N.,Fox, E.P.,Earnest, T.,Moon, R.T.
Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK signaling, is required for notochord formation
Dev.Cell, 2:449-461, 2002
Cited by
PubMed Abstract: 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.
PubMed: 11970895
DOI: 10.1016/S1534-5807(02)00140-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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