divalent cations and redox conditions regulate the molecular structure and function of visinin-like protein-1二价阳离子和氧化还原条件调节的分子结构和功能visinin-like蛋白1.pdfVIP

Divalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1 1 2 3 4 5 Conan K. Wang *, Anne Simon , Christian M. Jessen , Cristiano L. P. Oliveira , Lynsey Mack , 6 7 4 1,5 Karl-Heinz Braunewell , James B. Ames , Jan Skov Pedersen , Andreas Hofmann 1 Structural Chemistry Program, Eskitis Institute for Cell Molecular Therapies, Griffith University, Brisbane, Queensland, Australia, 2 Universite Lyon 1, Institut de Chimie ˜ ˜ et Biochimie Moleculaires et Supramoleculaires, Villeurbanne, France, 3 Complex Fluids Group, Department of Experimental Physics, University of Sao Paulo, Sao Paulo, Brazil, 4 Department of Chemistry and iNANO Interdisciplinary Nanoscience Centre, University of Aarhus, Aarhus, Denmark, 5 School of Biological Sciences, The University of Edinburgh, Edinburgh, Scotland, United Kingdom, 6 Molecular Cellular Neuroscience Laboratory, Biochemistry Molecular Biology Department, Southern Research Institute, Birmingham, Alabama, United States of America, 7 Department of Chemistry, University of California Davis, Davis, California, United States of America Abstract The NCS protein Visinin-like Protein 1 (VILIP-1) transduces calcium signals in the brain and serves as an effector of the non- retinal receptor guanylyl cyclases (GCs) GC-A and GC-B, and nicotinic acetyl choline receptors (nAchR). Analysis of the quaternary structure of VILIP-1 in solution reveals the existence