TY - JOUR
T1 - Structural studies of human Naked2
T2 - A biologically active intrinsically unstructured protein
AU - Hu, Tianhui
AU - Krezel, Andrzej M.
AU - Li, Cunxi
AU - Coffey, Robert J.
N1 - Funding Information:
We thank James Goldenring, Yuan Cheng, Ju Zhao, M Sundaramoothy, Susan Meyn, and Laura Mizoue for helpful discussions. This work was supported by National Institute of Health Grants 5R01CA046413, 5P50CA095103 (R.J.C.), and a National Institute of Health training Grant 5T32HL007751 (T.H.).
PY - 2006/12/1
Y1 - 2006/12/1
N2 - 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-α (TGFα) and escorts TGFα-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.
AB - 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-α (TGFα) and escorts TGFα-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.
KW - Circular dichroism
KW - Intrinsically unstructured protein
KW - Naked2
KW - Nuclear magnetic resonance
KW - Transforming growth factor-α
UR - https://www.scopus.com/pages/publications/33750060721
U2 - 10.1016/j.bbrc.2006.09.121
DO - 10.1016/j.bbrc.2006.09.121
M3 - Article
C2 - 17045239
AN - SCOPUS:33750060721
SN - 0006-291X
VL - 350
SP - 911
EP - 915
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -