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1ido

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[[Image:1ido.gif|left|200px]]<br />
 
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<applet load="1ido" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ido, resolution 1.7&Aring;" />
 
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'''I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND'''<br />
 
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==Overview==
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==I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND==
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We have determined the high resolution crystal structure of the A domain, from the alpha chain of integrin CR3. The domain adopts a classic, alpha/beta "Rossmann" fold and contains an unusual Mg2+ coordination site, at its surface. One of the coordinating ligands is the glutamate side, chain from another A domain molecule. We suggest that this site represents, a general metal ion-dependent adhesion site (MIDAS) for binding protein, ligands. We further propose that the beta subunits of integrins contain a, MIDAS motif within a modified A domain. Our crystal structure will allow, reliable models to be built for other members of the A domain superfamily, and should facilitate development of novel adhesion modulatory drugs.
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<StructureSection load='1ido' size='340' side='right'caption='[[1ido]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ido]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ido FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ido OCA], [https://pdbe.org/1ido PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ido RCSB], [https://www.ebi.ac.uk/pdbsum/1ido PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ido ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ITAM_HUMAN ITAM_HUMAN] Genetic variations in ITGAM has been associated with susceptibility to systemic lupus erythematosus type 6 (SLEB6) [MIM:[https://omim.org/entry/609939 609939]. Systemic lupus erythematosus (SLE) is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue. It affects principally the skin, joints, kidneys and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system.
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== Function ==
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[https://www.uniprot.org/uniprot/ITAM_HUMAN ITAM_HUMAN] Integrin alpha-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1ido_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ido ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IDO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: MG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDO OCA].
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*[[Integrin 3D structures|Integrin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)., Lee JO, Rieu P, Arnaout MA, Liddington R, Cell. 1995 Feb 24;80(4):631-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7867070 7867070]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lee, J.O.]]
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[[Category: Lee J-O]]
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[[Category: Liddington, R.]]
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[[Category: Liddington R]]
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[[Category: MG]]
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[[Category: cell adhesion protein]]
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[[Category: cytoskeleton]]
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[[Category: extracellular matrix]]
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[[Category: glycoprotein]]
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[[Category: integrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:29:00 2007''
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Current revision

I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND

PDB ID 1ido

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