Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
FEBS Lett. 2012 Sep 21;586(19):3122-6. doi: 10.1016/j.febslet.2012.07.072. Epub 2012 Aug 8.
A Wnt-binding site of the WIF-domain of Wnt inhibitory factor-1 was localized by structure-guided arginine-scanning mutagenesis in combination with surface plasmon resonance assays. Our observation that substitution of some residues of WIF resulted in an increased affinity for Wnt5a, but decreased affinity for Wnt3a, suggests that these residues may define the specificity spectrum of WIF for Wnts. These results hold promise for a more specific targeting of Wnt family members with WIF variants in various forms of cancer.
通过结构导向的精氨酸扫描突变结合表面等离子体共振分析，定位了 Wnt 抑制因子-1 的 WIF 结构域的 Wnt 结合位点。我们的观察结果表明，WIF 的一些残基的取代导致对 Wnt5a 的亲和力增加，但对 Wnt3a 的亲和力降低，这表明这些残基可能定义了 WIF 对 Wnt 的特异性谱。这些结果为使用 WIF 变体在各种形式的癌症中更特异性地靶向 Wnt 家族成员提供了希望。
