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dc.contributor.author
Saldaño, Tadeo Enrique
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dc.contributor.author
Tosatto, Silvio C. E.
dc.contributor.author
Parisi, Gustavo Daniel
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dc.contributor.author
Fernández Alberti, Sebastián
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dc.date.available
2022-07-07T13:55:41Z
dc.date.issued
2019-07
dc.identifier.citation
Saldaño, Tadeo Enrique; Tosatto, Silvio C. E.; Parisi, Gustavo Daniel; Fernández Alberti, Sebastián; Network analysis of dynamically important residues in protein structures mediating ligand-binding conformational changes; Springer; European Biophysics Journal With Biophysics Letters; 48; 6; 7-2019; 559-568
dc.identifier.issn
0175-7571
dc.identifier.uri
http://hdl.handle.net/11336/161557
dc.description.abstract
According to the generalized conformational selection model, ligand binding involves the co-existence of at least two conformers with different ligand-affinities in a dynamical equilibrium. Conformational transitions between them should be guaranteed by intramolecular vibrational dynamics associated to each conformation. These motions are, therefore, related to the biological function of a protein. Positions whose mutations are found to alter these vibrations the most can be defined as key positions, that is, dynamically important residues that mediate the ligand-binding conformational change. In a previous study, we have shown that these positions are evolutionarily conserved. They correspond to buried aliphatic residues mostly localized in regular structured regions of the protein like β-sheets and α-helices. In the present paper, we perform a network analysis of these key positions for a large dataset of paired protein structures in the ligand-free and ligand-bound form. We observe that networks of interactions between these key positions present larger and more integrated networks with faster transmission of the information. Besides, networks of residues result that are robust to conformational changes. Our results reveal that the conformational diversity of proteins seems to be guaranteed by a network of strongly interconnected key positions rather than individual residues.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
LIGAND-BINDING
dc.subject
PROTEIN CONFORMATIONAL CHANGES
dc.subject
RESIDUE INTERACTION NETWORKS
dc.subject
VIBRATIONAL NORMAL MODES
dc.subject.classification
Otras Ciencias Naturales y Exactas
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dc.subject.classification
Otras Ciencias Naturales y Exactas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Network analysis of dynamically important residues in protein structures mediating ligand-binding conformational changes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-07-07T13:47:51Z
dc.journal.volume
48
dc.journal.number
6
dc.journal.pagination
559-568
dc.journal.pais
Alemania
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dc.description.fil
Fil: Saldaño, Tadeo Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Tosatto, Silvio C. E.. Università di Padova; Italia
dc.description.fil
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Fernández Alberti, Sebastián. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
dc.journal.title
European Biophysics Journal With Biophysics Letters
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00249-019-01384-1
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00249-019-01384-1
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