Docking of Fatty Acids into the WIF Domain of the Human Wnt Inhibitory Factor-1

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. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

基于WIF的身份联合管理的研究

随着信息化系统规划和部署在业务领域的饱和度不断提升,面向业务的各种平台化应用消化并积聚了大量冗余的身份信息,使得单一用户要不断适应并辗转在几乎一直处于进化状态的体系丛林。同时,身份数据在应用中的冗余并没有恰如其分的建立诸如副本和镜像的联系,增加了维护成本和信息不对称的技术风险,建立职责化的统一身份标识库,让用户不再设置和管理重复的账户是十分必要的。本文介绍了基于WIF的身份联合管理技术的现状、应用研究和实现方法。