2D3J

NMR structure of the WIF domain from human WIF-1

Summary for 2D3J

Entry DOI	10.2210/pdb2d3j/pdb
Descriptor	Wnt inhibitory factor-1 (1 entity in total)
Functional Keywords	palmitoyl group, recognition domain, signaling protein inhibitor
Biological source	Homo sapiens (human)
Cellular location	Secreted: Q9Y5W5
Total number of polymer chains	1
Total formula weight	17511.96
Authors	Liepinsh, E.,Banyai, L.,Patthy, L.,Otting, G. (deposition date: 2005-09-29, release date: 2006-04-25, Last modification date: 2024-10-16)
Primary citation	Liepinsh, E.,Banyai, L.,Patthy, L.,Otting, G. NMR structure of the WIF domain of the human Wnt-inhibitory factor-1 J.Mol.Biol., 357:942-950, 2006 Cited by PubMed Abstract: 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. PubMed: 16476441 DOI: 10.1016/j.jmb.2006.01.047 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation