The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pone.0074383 (literal)

Alternative label

• Bellucci L.; Corni S.; Di Felice R.; Paci E. (2013)
  The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations
  in PloS one
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Bellucci L.; Corni S.; Di Felice R.; Paci E. (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-84884764317&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 8 (literal)

Rivista

• PloS one (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 9 (literal)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Center S3, CNR Institute Nanoscience, Modena, Italy; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom (literal)

Titolo

• The Structure of Neuronal Calcium Sensor-1 in Solution Revealed by Molecular Dynamics Simulations (literal)

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. (literal)

Prodotto di

• Nanobiosistemi (MD.P06.010.002) (Modulo)

Autore CNR

• STEFANO CORNI (Persona)
• ROSA DI FELICE (Persona)
• LUCA BELLUCCI (Persona)

Incoming links:

Autore CNR di

• ROSA DI FELICE (Persona)
• STEFANO CORNI (Persona)
• LUCA BELLUCCI (Persona)

Prodotto

• Nanobiosistemi (MD.P06.010.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PloS one (Rivista)