Structural studies of human Naked2: a biologically active intrinsically unstructured protein.

Hu T, Krezel AM, Li C, Coffey RJ
Biochem Biophys Res Commun. 2006 350 (4): 911-5

PMID: 17045239 · PMCID: PMC1661664 · DOI:10.1016/j.bbrc.2006.09.121

Naked1 and 2 are two mammalian orthologs of Naked Cuticle, a canonical Wnt signaling antagonist in Drosophila. Naked2, but not Naked1, interacts with transforming growth factor-alpha (TGFalpha) and escorts TGFalpha-containing vesicles to the basolateral membrane of polarized epithelial cells. Full-length Naked2 is poorly soluble. Since most functional domains, including the Dishevelled binding region, EF-hand, vesicle recognition, and membrane targeting motifs, reside in the N-terminal half of the protein, we expressed and purified the first 217 residues of human Naked2 and performed a functional analysis of this fragment. Its circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra showed no evidence of secondary and/or tertiary structure. The fragment did not bind calcium or zinc. These results indicate that the N-terminal half of Naked2 behaves as an intrinsically unstructured protein.

MeSH Terms (7)

Amino Acid Sequence Carrier Proteins Humans Molecular Conformation Protein Conformation Solubility Wnt Proteins

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