2d3j
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3j OCA], [http://www.ebi.ac.uk/pdbsum/2d3j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d3j RCSB]</span> | ||
}} | }} | ||
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[[Category: recognition domain]] | [[Category: recognition domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:49 2008'' |
Revision as of 23:29, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of the WIF domain from human WIF-1
Overview
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.
About this Structure
2D3J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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