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[[Image:1ido.gif|left|200px]]


{{Structure
==I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND==
|PDB= 1ido |SIZE=350|CAPTION= <scene name='initialview01'>1ido</scene>, resolution 1.7&Aring;
<StructureSection load='1ido' size='340' side='right'caption='[[1ido]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=MG:Metal+Binding+Site.+This+Site+Also+Includes+GLU+314+From+...'>MG</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ido FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ido OCA], [http://www.ebi.ac.uk/pdbsum/1ido PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ido RCSB]</span>
== Disease ==
}}
[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.
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1ido_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND'''
==See Also==
 
*[[Integrin 3D structures|Integrin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1IDO is a [[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=1IDO OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/7867070 7867070]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Lee, J O.]]
[[Category: Lee J-O]]
[[Category: Liddington, R.]]
[[Category: Liddington R]]
[[Category: cell adhesion protein]]
[[Category: cytoskeleton]]
[[Category: extracellular matrix]]
[[Category: glycoprotein]]
[[Category: integrin]]
 
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Retrieved from "https://proteopedia.org/1ido"