Structural highlights
Function
[WIF1_HUMAN] Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The human Wnt-binding protein Wnt-inhibitory factor-1 (WIF-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 beta-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.
NMR structure of the WIF domain of the human Wnt-inhibitory factor-1.,Liepinsh E, Banyai L, Patthy L, Otting G J Mol Biol. 2006 Mar 31;357(3):942-50. Epub 2006 Jan 31. PMID:16476441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liepinsh E, Banyai L, Patthy L, Otting G. NMR structure of the WIF domain of the human Wnt-inhibitory factor-1. J Mol Biol. 2006 Mar 31;357(3):942-50. Epub 2006 Jan 31. PMID:16476441 doi:10.1016/j.jmb.2006.01.047
