A new member of the discoidin family: in silico analysis of Paracentrotus lividus nectin based on its cDNA sequence (Abstract/Poster in atti di convegno)

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  • A new member of the discoidin family: in silico analysis of Paracentrotus lividus nectin based on its cDNA sequence (Abstract/Poster in atti di convegno) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Alternative label
  • Costa C; Zito F; Matranga V (2009)
    A new member of the discoidin family: in silico analysis of Paracentrotus lividus nectin based on its cDNA sequence
    in FISV, Riva del Garda (TN), 23-25 settembre 2009
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Costa C; Zito F; Matranga V (literal)
Note
  • Abstract (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR - IBIM- Istituto di Biomedicina e Immunologia Molecolare \"Alberto Monroy\" - Via Ugo La Malfa 153, 90146 Palermo, Italy (literal)
Titolo
  • A new member of the discoidin family: in silico analysis of Paracentrotus lividus nectin based on its cDNA sequence (literal)
Abstract
  • We obtained the cDNA sequence coding for Pl-nectin, an extracellular matrix protein purified from the sea urchin, composed of two 105 kDa equivalent subunits. The protein, synthesized as a 984aa precursor containing a 23aa signal peptide, is a new member of the galactose-binding protein superfamily. In fact, it consists of six 151-156aa-long tandemly-repeated domains, which are homologous to the discoidin-like domains, also known as F5/8 Type C domains. Phylogenetic analysis with discoidin domains from other known proteins confirmed the importance of their biological role during evolution. In addition, we describe the three-dimensional structure for each Pl-nectin domain, obtained on the basis of the homology modelling with crystal structures of the human coagulation factor V and VIII C2 domains and neuropilin-1 b1 domain. A further two-domains modelling and the subsequent association of the three two-domains modelled dimers produced the assembled Pl-nectin subunit. The in silico quaternary structure of the two subunits, composed of two 105kDa C-shaped monomers linked by a disulfide bridge accounts for the whole 210 kDa Pl-nectin molecule. The model presented is consistent with earlier biochemical reports on the molecule and extends previous conclusions concerning its function. In addition, the in silico analysis offers a basis for predictions to be experimentally tested. (literal)
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