The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1. (Articolo in rivista)

Type
Label
  • The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1. (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jmb.2007.01.011 (literal)
Alternative label
  • Márquez JA; Galfré E; Dupeux F; Flot D; Moran O; Dimasi N. (2007)
    The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1.
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Márquez JA; Galfré E; Dupeux F; Flot D; Moran O; Dimasi N. (literal)
Pagina inizio
  • 310 (literal)
Pagina fine
  • 318 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 367 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • EMBL, Istituto di Biofisica, Istituto Giannina Gaslini (literal)
Titolo
  • The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1. (literal)
Abstract
  • The immune receptors expressed on myeloid cells (IREM) are type I transmembrane proteins encoded on human chromosome 17 (17q25.1), whose function is believed to be important in controlling inflammation. To date, three IREM receptors have been identified. IREM-1 functions as an inhibitory receptor, whereas IREM-2 and IREM-3 serve an activating function. Here, we report the crystal structure of IREM-1 extracellular domain at 2.6 A resolution. The overall fold of IREM-1 resembles that of a V-type immunoglobulin domain, and reveals overall close homology with immunoglobulin domains from other immunoreceptors such as CLM-1, TREM-1, TLT-1 and NKp44. Comparing the surface electrostatic potential and hydrophobicity of IREM-1 with its murine homologous CLM-1, we observed unique structural properties for the complementary determining region of IREM-1, which suggests that they may be involved in recognition of the IREM-1 ligand. Particularly interesting is the structural conformation and physical properties of the antibody's equivalent CDR3 loop, which we show to be a structurally variable region of the molecule and therefore could be the main structural determinant for ligand discrimination and binding. In addition, the analysis of the IREM-1 structure revealed the presence of four structurally different cavities. Three of these cavities form a continuous hydrophobic groove on the IREM-1 surface, which point to a region of the molecule capable of accommodating potential ligands. (literal)
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