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. © 2013 Bellucci et al.

Bellucci L., Corni S., Di Felice R., Paci E. (2013). The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations. PLOS ONE, 8(9), e74383-10 [10.1371/journal.pone.0074383].

The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations

Paci E.
2013

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. © 2013 Bellucci et al.
2013
Bellucci L., Corni S., Di Felice R., Paci E. (2013). The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations. PLOS ONE, 8(9), e74383-10 [10.1371/journal.pone.0074383].
Bellucci L.; Corni S.; Di Felice R.; Paci E.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/885204
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