2nms: Difference between revisions

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caption="2nms, resolution 2.60Å" />

'''The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2NMS OCA].

2NMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NMS 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17275839 17275839]

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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17275839 17275839]

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Dimasi, N.]]

[[Category: Marquez, J.A.]]

[[Category: Marquez, J A.]]

[[Category: ig-superfamily]]

[[Category: ig-v]]

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[[Category: nkp44-like]]

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-[[Image:2nms.gif|left|200px]]<br />
+[[Image:2nms.gif|left|200px]]<br /><applet load="2nms" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2nms" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2nms, resolution 2.60&Aring;" />
 '''The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1'''<br />
 ==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.
+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==
-NMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NMS OCA].
+NMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NMS 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17275839 17275839]
+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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17275839 17275839]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
 [[Category: Dimasi, N.]]
-[[Category: Marquez, J.A.]]
+[[Category: Marquez, J A.]]
 [[Category: ig-superfamily]]
 [[Category: ig-v]]
@@ Line 25: / Line 24: @@
 [[Category: nkp44-like]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:59:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:31 2008''