http://www.cnr.it/ontology/cnr/individuo/prodotto/ID272934
THE STRUCTURE OF THE CD3 ZZ TRANSMEMBRANE DIMER IN POPC AND RAFT-LIKE LIPID BILAYER: A MOLECULAR DYNAMICS APPROACH. (Articolo in rivista)
- Type
- Label
- THE STRUCTURE OF THE CD3 ZZ TRANSMEMBRANE DIMER IN POPC AND RAFT-LIKE LIPID BILAYER: A MOLECULAR DYNAMICS APPROACH. (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/J.BBAMEM.2013.07.019 (literal)
- Alternative label
Ariel Alcides Petruka, Sonia Varriale, Maria Rosaria Coscia, Lelio Mazzarellab, Antonello Merlino, Umberto Oreste. (2013)
THE STRUCTURE OF THE CD3 ZZ TRANSMEMBRANE DIMER IN POPC AND RAFT-LIKE LIPID BILAYER: A MOLECULAR DYNAMICS APPROACH.
in Elsevier science
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ariel Alcides Petruka, Sonia Varriale, Maria Rosaria Coscia, Lelio Mazzarellab, Antonello Merlino, Umberto Oreste. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Instituto Superior de Investigaciones Biológicas (INSIBIO-CONICET), Chacabuco 461, S. M. de Tucumán, Tucumán T4000ILI, Argentina
Department of Chemical Sciences, University of Naples \"Federico II\", via Cintia, 80126 Napoli, Italy
Institute of Protein Biochemistry, CNR, via P. Castellino 111, 80131 Napoli, Italy
Institute of Biostructures and Bioimages, CNR, via Mezzocannone 16, 80100 Napoli, Italy (literal)
- Titolo
- THE STRUCTURE OF THE CD3 ZZ TRANSMEMBRANE DIMER IN POPC AND RAFT-LIKE LIPID BILAYER: A MOLECULAR DYNAMICS APPROACH. (literal)
- Abstract
- Plasma membrane lipids significantly affect assembly and activity of many signaling networks. The present work is aimed at analyzing, by molecular dynamics simulations, the structure and dynamics of the CD3 ?? dimer in palmitoyl-oleoyl-phosphatidylcholine bilayer (POPC) and in POPC/cholesterol/sphingomyelin bilayer, which resembles the raft membrane microdomain supposed to be the site of the signal transducing machinery. Both POPC and raft-like environment produce significant alterations in structure and flexibility of the CD3 ?? with respect to nuclear magnetic resonance (NMR) model: the dimer is more compact, its secondary structure is slightly less ordered, the arrangement of the Asp6 pair, which is important for binding to the Arg residue in the alpha chain of the T cell receptor (TCR), is stabilized by water molecules. Different interactions of charged residues with lipids at the lipid-cytoplasm boundary occur when the two environments are compared. Furthermore, in contrast to what is observed in POPC, in the raft-like environment correlated motions between transmembrane and cytoplasmic regions are observed. Altogether the data suggest that when the TCR complex resides in the raft domains, the CD3 ?? dimer assumes a specific conformation probably necessary to the correct signal transduction. (literal)
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Insieme di parole chiave di