ArticlePloS one2013
The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Aptamer-based gold nanoparticle aggregates for ultrasensitive amplification-free detection of PSMA.Scientific reports · 2023Article
- Distinct mechanism of TbPhysical chemistry chemical physics : PCCP · 2023Article
- Disorder in a two-domain neuronal CaCellular and molecular life sciences : CMLS · 2021Article
- Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality.ACS central science · 2017Article
- Human Neuronal Calcium Sensor-1 Protein Avoids Histidine Residues To Decrease pH Sensitivity.The journal of physical chemistry. B · 2017Article
- Temperature-Dependent Conformational Properties of Human Neuronal Calcium Sensor-1 Protein Revealed by All-Atom Simulations.The journal of physical chemistry. B · 2016Article
- Effects of the C-Terminal Tail on the Conformational Dynamics of Human Neuronal Calcium Sensor-1 Protein.The journal of physical chemistry. B · 2015Article
- Single-molecule folding mechanisms of the apo- and Mg(2+)-bound states of human neuronal calcium sensor-1.Biophysical journal · 2015Article
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Authors and funding
4 authors.
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Abstract
Neuronal calcium sensor-1 (NCS-1) is a protein able to trigger signal transduction processes by binding a large number of substrates and re-shaping its structure depending on the environmental conditions. The X-ray crystal structure of the unmyristoilated NCS-1 shows a large solvent-exposed hydrophobic crevice (HC); this HC is partially occupied by the C-terminal tail and thus elusive to the surrounding solvent. We studied the native state of NCS-1 by performing room temperature molecular dynamics (MD) simulations starting from the crystal and the solution structures. We observe relaxation to a state independent of the initial structure, in which the C-terminal tail occupies the HC. We suggest that the C-terminal tail shields the HC binding pocket and modulates the affinity of NCS-1 for its natural targets. By analyzing the topology and nature of the inter-residue potential energy, we provide a compelling description of the interaction network that determines the three-dimensional organization of NCS-1.
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