期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 357, 期 3, 页码 942-950出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.01.047
关键词
WIF domain; NMR spectroscopy; three-dimensional structure; Wnt; palmitoylation
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.
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