1HCE

STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR

1HCE の概要

• エントリーDOI: 10.2210/pdb1hce/pdb
• 分子名称: HISACTOPHILIN (1 entity in total)
• 機能のキーワード: actin binding
• 由来する生物種: Dictyostelium discoideum
• 細胞内の位置: Cytoplasm: P13231
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13496.91

構造登録者

Habazettl, J.,Gondol, D.,Wiltscheck, R.,Otlewski, J.,Schleicher, M.,Holak, T.A. (登録日: 1994-07-12, 公開日: 1994-09-30, 最終更新日: 2024-05-01)

主引用文献

Habazettl, J.,Gondol, D.,Wiltscheck, R.,Otlewski, J.,Schleicher, M.,Holak, T.A.
Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.
Nature, 359:855-858, 1992

PubMed Abstract: The fast reaction of the actin-based cytoskeleton in motile cells after stimulation with a chemoattractant requires a signal-transduction chain that creates a very specific environment at distinct regions beneath the plasma membrane. Dictyostelium hisactophilin, a unique actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerization and binding to microfilaments only at pH values below seven. It has a relative molecular mass of 13.5K and its most unusual feature is the presence of 31 histidine residues among its total of 118 amino acids. The transduction of an external signal from the plasma membrane to the cytoskeleton is poorly understood. Here we report the protein's structure in solution determined by nuclear magnetic resonance spectroscopy. The nuclear Overhauser effect intensities of the three-dimensional nuclear Overhauser spectra were used directly in the calculations. The overall folding of histactophilin is similar to that of interleukin-1 beta and fibroblast growth factor, but the primary amino-acid sequence of hisactophilin is unrelated to these two proteins.

PubMed: 1436061
DOI: 10.1038/359855a0

実験手法

SOLUTION NMR