期刊
FEBS LETTERS
卷 589, 期 20, 页码 3044-3051出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.08.031
关键词
Arginine-scanning mutagenesis; Cancer therapy; Homology modeling; Protein-protein interaction; Ryk receptor tyrosine kinase; WIF domain; Wnt; Wnt Inhibitory Factor 1
资金
- OTKA (National Scientific Research Fund of Hungary, OTKA) [K75836]
- ETT (Medical Research Council, Hungary) [001-07/2009]
Wnts have a structure resembling a hand with thumb and index fingers that grasp the cysteine rich domains of Frizzled receptors at two distinct binding sites. In the present work we show that the WIF domain of Wnt Inhibitory Factor 1 is also bound by Wnts at two sites. Using C-terminal domains of Wnt5a and Wnt7a and arginine-scanning mutagenesis of the WIF domain we demonstrate that, whereas the N-terminal, lipid-modified thumb of Wnts interacts with the alkyl-binding site of the WIF domain, the C-terminal domain of Writs (Wnt-CTD) binds to a surface on the opposite side of the WIF domain. (C) 2015 The Authors. Published by Elsevier B.V.
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