ArticlePloS one2016
Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Transcriptomic Profiling of Orbital Fat Tissue and Ocular Surface Wash in Active Thyroid Eye Disease Requiring Urgent Orbital Decompression.Investigative ophthalmology & visual science · 2025Article
- Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue.Journal of the American Chemical Society · 2023Article
- Expressional and prognostic value of HPCAL1 in cholangiocarcinoma via integrated bioinformatics analyses and experiments.Cancer medicine · 2023Article
- N-Myristoyltransferase as a Glycine and Lysine Myristoyltransferase in Cancer, Immunity, and Infections.ACS chemical biology · 2020Review
- A Novel Approach to Bacterial Expression and Purification of Myristoylated Forms of Neuronal Calcium Sensor Proteins.Biomolecules · 2020Article
- Quantitative Determination of CaBio-protocol · 2020Article
- Effects of Membrane and Biological Target on the Structural and Allosteric Properties of Recoverin: A Computational Approach.International journal of molecular sciences · 2019Article
- Dimerization of Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2018Review
- Interference of the complex between NCS-1 and Ric8a with phenothiazines regulates synaptic function and is an approach for fragile X syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
4 authors.
Funding
Abstract
Visinin-like protein 3 (VILIP-3) belongs to a family of Ca2+-myristoyl switch proteins that regulate signal transduction in the brain and retina. Here we analyze Ca2+ binding, characterize Ca2+-induced conformational changes, and determine the NMR structure of myristoylated VILIP-3. Three Ca2+ bind cooperatively to VILIP-3 at EF2, EF3 and EF4 (KD = 0.52 μM and Hill slope of 1.8). NMR assignments, mutagenesis and structural analysis indicate that the covalently attached myristoyl group is solvent exposed in Ca2+-bound VILIP-3, whereas Ca2+-free VILIP-3 contains a sequestered myristoyl group that interacts with protein residues (E26, Y64, V68), which are distinct from myristate contacts seen in other Ca2+-myristoyl switch proteins. The myristoyl group in VILIP-3 forms an unusual L-shaped structure that places the C14 methyl group inside a shallow protein groove, in contrast to the much deeper myristoyl binding pockets observed for recoverin, NCS-1 and GCAP1. Thus, the myristoylated VILIP-3 protein structure determined in this study is quite different from those of other known myristoyl switch proteins (recoverin, NCS-1, and GCAP1). We propose that myristoylation serves to fine tune the three-dimensional structures of neuronal calcium sensor proteins as a means of generating functional diversity.
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