Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin (Articolo in rivista)

Type
Label
  • Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s11030-009-9203-3 (literal)
Alternative label
  • Costa, Caterina; Cavalcante, Carmela; Zito, Francesca; Yokota, Yukio; Matranga, Valeria (2010)
    Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin
    in Molecular diversity (Dordr., Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Costa, Caterina; Cavalcante, Carmela; Zito, Francesca; Yokota, Yukio; Matranga, Valeria (literal)
Pagina inizio
  • 653 (literal)
Pagina fine
  • 665 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 14 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • Mol Divers. 2009 Nov 12. [Epub ahead of print] PubMed PMID: 19908157. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 4 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR -- Consiglio Nazionale delle Ricerche - IBIM - Istituto di biomedicina e di immunologia molecolare Y. Yokota Department of Applied Information Science and Technology, Aichi Prefectural University, Nagakute, Aichi 480-1198, Japan (literal)
Titolo
  • Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin (literal)
Abstract
  • The extracellular matrix protein Pl-nectin, a 210-kDa homodimer originally purified from sea urchin eggs, plays a crucial role in cell adhesion and embryonic morphogenesis. The compiled cDNA sequence, obtained by RT-PCR primer walking and 3? RACE, identified a 984aa product containing a 23aa signal peptide and including all six internal peptides identified by protein microsequencing. The protein is a new member of the galactose-binding protein superfamily as it consists of six 151-156aa-long tandemly repeated domains (D1-D6), homologous to the discoidin-like domains, also known as F5/8-type C domains. Based on homology modelling, we present a three-dimensional structure (3D) for D5, identified as the prototype domain. The molecular modelling of the assembled Pl-nectin homodimer accounts for a Pl-nectin quaternary structure composed of two 105-kDa C-shaped monomers linked by a S-S bridge. The presence of an LDT motif between the first and the second exposed loops of the D2 domain suggests the binding of Pl-nectin to an integrin receptor. Altogether, the in silico analysis described here is consistent with previous biochemical reports and offers a basis for predictions to be experimentally tested. (literal)
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