8e0w
From Proteopedia
Crystal structure of mouse APCDD1 in P1 space group
Structural highlights
FunctionAPCD1_MOUSE Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin. May act via its interaction with Wnt and LRP proteins (By similarity). Publication Abstract from PubMedDiverse extracellular proteins negatively regulate WNT signaling. One such regulator is adenomatosis polyposis coli down-regulated 1 (APCDD1), a conserved single-span transmembrane protein. In response to WNT signaling in a variety of tissues, APCDD1 transcripts are highly up-regulated. We have determined the three-dimensional structure of the extracellular domain of APCDD1, and this structure reveals an unusual architecture consisting of two closely apposed beta-barrel domains (ABD1 and ABD2). ABD2, but not ABD1, has a large hydrophobic pocket that accommodates a bound lipid. The APCDD1 ECD can also bind to WNT7A, presumably via its covalently bound palmitoleate, a modification that is common to all WNTs and is essential for signaling. This work suggests that APCDD1 functions as a negative feedback regulator by titrating WNT ligands at the surface of responding cells. Structure of WNT inhibitor adenomatosis polyposis coli down-regulated 1 (APCDD1), a cell-surface lipid-binding protein.,Hsieh FL, Chang TH, Gabelli SB, Nathans J Proc Natl Acad Sci U S A. 2023 May 16;120(20):e2217096120. doi: , 10.1073/pnas.2217096120. Epub 2023 May 8. PMID:37155902[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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