Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1
Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1
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DOI：
10.1007/s11745-007-3144-3
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发表时间：
2008-03-01
期刊：
影响因子：
1.9
通讯作者：
Malinauskas, Tomas
中科院分区：
文献类型：
--
作者：
Malinauskas, Tomas
棕榈酰化Wnt蛋白包含与多种人类癌症相关的分泌信号分子的保守家族。人WIF（Wnt抑制因子）-1的WIF结构域足以用于Wnt结合和信号传导抑制。Wnt和WIF-1之间的详细相互作用尚不清楚。采用计算对接来确定WIF结构域中可能的脂肪酸结合位点。一个推定的结合位点内确定的结构域。WIF结构域对C16：0-C18：0（~ 22 kJ/mol结合自由能）脂肪酸表现出最高的亲和力。结果表明WIF结构域作为WIF-1与棕榈酰化Wnt结合和信号传导抑制所需的棕榈酰结合结构域的作用。
Palmitoylated Wnt proteins comprise a conserved family of secreted signaling molecules associated with variety of human cancers. WIF domain of the human WIF (Wnt inhibitory factor)-1 is sufficient for Wnt binding and signaling inhibition. Detailed interactions between Wnt and WIF-1 are not known. Computational docking was employed to identify a possible fatty acid binding site in the WIF domain. A putative binding site was identified inside the domain. WIF domain exhibited the highest affinity for C16:0-C18:0 (-22 kJ/mol free energy of binding) fatty acids. The results suggest a role of the WIF domain as a palmitoyl binding domain required for WIF-1 binding to palmitoylated Wnt and signaling inhibition.