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| | {{STRUCTURE_2nms| PDB=2nms | SCENE= }} | | {{STRUCTURE_2nms| PDB=2nms | SCENE= }} |
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| - | '''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=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17275839}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17275839 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17275839}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Negative regulation of leukocyte]] | | [[Category: Negative regulation of leukocyte]] |
| | [[Category: Nkp44-like]] | | [[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 Tue Jul 29 14:06:05 2008'' |
Revision as of 11:06, 29 July 2008
Template:STRUCTURE 2nms
The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1
Template:ABSTRACT PUBMED 17275839
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
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