NMR structure of the WIF domain of the human Wnt-inhibitory factor-1
NMR structure of the WIF domain of the human Wnt-inhibitory factor-1
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DOI：
10.1016/j.jmb.2006.01.047
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发表时间：
2006-03-31
影响因子：
5.6
通讯作者：
Otting, G
中科院分区：
文献类型：
--
作者：
Liepinsh, E;Bányai, L;Otting, G
人Wnt结合蛋白Wnt抑制因子-1（Wnt-1）包含N-末端WIF模块，随后是五个EGF样重复。在这里，我们报告的三维结构的WIF域的WIF-1的NMR光谱确定的折叠由一个八链三明治让人想起免疫球蛋白折叠。发现在重折叠方案中使用的残留去污剂（Brij-35）与WIF结构域紧密结合。结合位点通过在WIF结构域和洗涤剂的烷基链之间观察到的分子间核Overhauser效应来鉴定。结果表明，WIF结构域作为Wnt和果蝇Hedgehog蛋白的识别基序，通过棕榈酰化激活可能发挥作用。(c)2006爱思唯尔有限公司保留所有权利。
The human Wnt-binding protein Wnt-inhibitory factor-1 (WIP-1) comprises an N-terminal WIF module followed by five EGF-like repeats. Here we report the three-dimensional structure of the WIF domain of WIF-1 determined by NMR spectroscopy The fold consists of an eight-stranded sandwich reminiscent of the immunoglobulin fold. Residual detergent (Brij-35) used in the refolding protocol was found to bind tightly to the WIF domain. The binding site was identified by intermolecular nuclear Overhauser effects observed between the WIF domain and the alkyl chain of the detergent. The results point to a possible role of WIF domains as a recognition motif of Wnt and Drosophila Hedgehog proteins that are activated by palmitoylation. (c) 2006 Elsevier Ltd. All rights reserved.