2D3J

NMR structure of the WIF domain from human WIF-1

2D3J の概要

• エントリーDOI: 10.2210/pdb2d3j/pdb
• 分子名称: Wnt inhibitory factor-1 (1 entity in total)
• 機能のキーワード: palmitoyl group, recognition domain, signaling protein inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: Q9Y5W5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17511.96

構造登録者

Liepinsh, E.,Banyai, L.,Patthy, L.,Otting, G. (登録日: 2005-09-29, 公開日: 2006-04-25, 最終更新日: 2024-10-16)

主引用文献

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

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

実験手法

SOLUTION NMR