8e0p

Crystal structure of mouse APCDD1 in fusion with engineered MBP

spinqualitylabelsall models 8e0p, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e0p is a 4 chain structure with sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.33Å Ligands: BGC, CL, DMX, GLC, GOL, NAG, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C3SHQ8_ECOLX Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins.[RuleBase:RU365005]APCD1_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 PubMed Diverse 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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