http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17780
A second Ig-like domain identified in dystroglycan by molecular modelling and dynamics (Articolo in rivista)
- Type
- Label
- A second Ig-like domain identified in dystroglycan by molecular modelling and dynamics (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jmgm.2011.04.008 (literal)
- Alternative label
De Rosa, Maria Cristina; Pirolli, Davide; Bozzi, Manuela; Sciandra, Francesca; Giardina, Bruno; Brancaccio, Andrea (2011)
A second Ig-like domain identified in dystroglycan by molecular modelling and dynamics
in Journal of molecular graphics & modelling
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- De Rosa, Maria Cristina; Pirolli, Davide; Bozzi, Manuela; Sciandra, Francesca; Giardina, Bruno; Brancaccio, Andrea (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- ISI Web of Science (WoS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Catholic University of the Sacred Heart (literal)
- Titolo
- A second Ig-like domain identified in dystroglycan by molecular modelling and dynamics (literal)
- Abstract
- Dystroglycan (DG) is a cell surface receptor which is composed of two subunits that interact noncovalently, namely alpha- and beta-DG. In skeletal muscle, DG is the central component of the dystrophin-glycoprotein complex (DGC) that anchors the actin cytoskeleton to the extracellular matrix. To date only the three-dimensional structure of the N-terminal region of alpha-DG has been solved by X-ray crystallography. To expand such a structural analysis, a theoretical molecular model of the murine alpha-DG C-terminal region was built based on folding recognition/threading techniques. Although there is no a significant (<30%) sequence homology with the N-terminal region of alpha-DG, protein fold recognition methods found a significant resemblance to the alpha-DG N-terminal crystallographic structure. Our in silico structural prediction identified two subdomains in this region. Amino acid residues similar to 500-600 of alpha-DG were predicted to adopt an immunoglobulin-like (Ig-like) beta-sandwich fold. Such modeled domain includes the beta-DG binding epitope of alpha-DG and, confirming our previous experimental results, suggests that the linear epitope (residues 550-565) assumes a beta-strand conformation. The remaining segment of the alpha-DG C-terminal region (residues 601-653) is organized in a coil-helix-coil motif. A 20-ns molecular dynamics simulation in explicit water solvent provided support to the predicted Ig-like model structure. The identification of a second Ig-like domain in DG represents another important step towards a full structural and functional description of the alpha/beta DG interface. Preliminary characterization of a novel recombinant peptide (505-600) encompassing this second lg-like domain demonstrates that it is soluble and stable, further corroborating our in silico analysis. (C) 2011 Elsevier Inc. All rights reserved. (literal)
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