Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering. (Articolo in rivista)

Type
Label
  • Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1529/biophysj.107.116590 (literal)
Alternative label
  • Moran O.; Roessle M.W.; Mariuzza R.A.; Dimasi N. (2008)
    Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering.
    in Biophysical journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Moran O.; Roessle M.W.; Mariuzza R.A.; Dimasi N. (literal)
Pagina inizio
  • 1766 (literal)
Pagina fine
  • 1772 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 94 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biofisica; EMBL; University of Maryland; Istituto Giannina Gaslini (literal)
Titolo
  • Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering. (literal)
Abstract
  • The Grb2-related adaptor protein GADS plays a central role during the initial phases of signal transduction in T lymphocytes. GADS possesses N- and C-terminal Src homology 3 (SH3) domains flanking a central Src homology 2 (SH2) domain and a 126-residue region rich in glutamine and proline residues, presumed to be largely unstructured. The SH2 domain of GADS binds the adaptor protein LAT; the C-terminal SH3 domain pairs GADS to the adaptor protein SLP-76, whereas the function of the central region is unknown. High-resolution three-dimensional models are available for the isolated SH2 and C-terminal SH3 domains in complex with their respective binding partners, LAT and SLP-76. However, in part because of its intrinsic instability, there is no structural information for the entire GADS molecule. Here, we report the low-resolution structure of full-length GADS in solution using small-angle x-ray scattering (SAXS). Based on the SAXS data, complemented by gel filtration experiments, we show that full-length GADS is monomeric in solution and that its overall structural parameters are smaller than those expected for a protein with a long unstructured region. Ab initio and rigid body modeling of the SAXS data reveal that full-length GADS is a relatively compact molecule and that the potentially unstructured region retains a significant degree of structural order. The biological function of GADS is discussed based on its overall structure. (literal)
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it