http://www.cnr.it/ontology/cnr/individuo/prodotto/ID200245
Molecular Mechanism of Allosteric Communication in Hsp70 Revealed by Molecular Dynamics Simulations (Articolo in rivista)
- Type
- Label
- Molecular Mechanism of Allosteric Communication in Hsp70 Revealed by Molecular Dynamics Simulations (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1371/journal.pcbi.1002844 (literal)
- Alternative label
Chiappori F., Merelli I., Colombo G., Milanesi L., Morra G. (2012)
Molecular Mechanism of Allosteric Communication in Hsp70 Revealed by Molecular Dynamics Simulations
in PLOS computational biology (Online)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Chiappori F., Merelli I., Colombo G., Milanesi L., Morra G. (literal)
- Pagina inizio
- Issue 12 e 1002844 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Tecnologie Biomediche, CNR - ICRM CNR (literal)
- Titolo
- Molecular Mechanism of Allosteric Communication in Hsp70 Revealed by Molecular Dynamics Simulations (literal)
- Abstract
- Investigating ligand-regulated allosteric coupling between protein domains is fundamental to understand cell-life
regulation. The Hsp70 family of chaperones represents an example of proteins in which ATP binding and hydrolysis at the
Nucleotide Binding Domain (NBD) modulate substrate recognition at the Substrate Binding Domain (SBD). Herein, a
comparative analysis of an allosteric (Hsp70-DnaK) and a non-allosteric structural homolog (Hsp110-Sse1) of the Hsp70
family is carried out through molecular dynamics simulations, starting from different conformations and ligand-states.
Analysis of ligand-dependent modulation of internal fluctuations and local deformation patterns highlights the structural
and dynamical changes occurring at residue level upon ATP-ADP exchange, which are connected to the conformational
transition between closed and open structures. By identifying the dynamically responsive protein regions and specific crossdomain
hydrogen-bonding patterns that differentiate Hsp70 from Hsp110 as a function of the nucleotide, we propose a
molecular mechanism for the allosteric signal propagation of the ATP-encoded conformational signal. (literal)
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