2nms
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2nms.gif|left|200px]] | [[Image:2nms.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2nms", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2nms| PDB=2nms | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1''' | '''The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1''' | ||
| Line 27: | Line 24: | ||
[[Category: Dimasi, N.]] | [[Category: Dimasi, N.]] | ||
[[Category: Marquez, J A.]] | [[Category: Marquez, J A.]] | ||
| - | [[Category: | + | [[Category: Ig-superfamily]] |
| - | [[Category: | + | [[Category: Ig-v]] |
| - | [[Category: | + | [[Category: Inhibitory receptor]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Myelo-monocytic cell]] |
| - | [[Category: | + | [[Category: Myeloid ig-like receptor]] |
| - | [[Category: | + | [[Category: Negative regulation of leukocyte]] |
| - | [[Category: | + | [[Category: Nkp44-like]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:38:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:38, 4 May 2008
The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1
Overview
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.
About this Structure
2NMS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1., Marquez JA, Galfre E, Dupeux F, Flot D, Moran O, Dimasi N, J Mol Biol. 2007 Mar 23;367(2):310-8. Epub 2007 Jan 10. PMID:17275839 Page seeded by OCA on Sun May 4 09:38:31 2008
