2NMS

The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1

Summary for 2NMS

• Entry DOI: 10.2210/pdb2nms/pdb
• Descriptor: CMRF35-like-molecule 1 (2 entities in total)
• Functional Keywords: ig-superfamily, ig-v, nkp44-like, myeloid ig-like receptor, inhibitory receptor, myelo-monocytic cells, negative regulation of leukocyte, membrane protein, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein (Potential): Q8TDQ1
• Total number of polymer chains: 1
• Total formula weight: 13976.71

Authors

Dimasi, N.,Marquez, J.A. (deposition date: 2006-10-23, release date: 2006-11-07, Last modification date: 2024-10-09)

Primary citation

Marquez, J.A.,Galfre, E.,Dupeux, F.,Flot, D.,Moran, O.,Dimasi, N.
The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1.
J.Mol.Biol., 367:310-318, 2007

PubMed 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.

PubMed: 17275839
DOI: 10.1016/j.jmb.2007.01.011

Experimental method

X-RAY DIFFRACTION (2.6 Å)