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1idn

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(New page: 200px<br /> <applet load="1idn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idn, resolution 2.7&Aring;" /> '''MAC-1 I DOMAIN METAL...)
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[[Image:1idn.gif|left|200px]]<br />
 
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<applet load="1idn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1idn, resolution 2.7&Aring;" />
 
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'''MAC-1 I DOMAIN METAL FREE'''<br />
 
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==Overview==
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==MAC-1 I DOMAIN METAL FREE==
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BACKGROUND: The integrin family of cell-surface receptors mediate cell, adhesion through interactions with the extracellular matrix or other, cell-surface receptors. The alpha chain of some integrin heterodimers, includes an inserted 'I domain' of about 200 amino acids which binds, divalent metal ions and is essential for integrin function. Lee et al., proposed that the I domain of the integrin CD11b adopts a unique 'active', conformation when bound to its counter receptor. In addition, they, proposed that the lack of adhesion in the presence of Ca2+ ion reflected, the stabilization of an 'inactive' I-domain conformation. We set out to, independently determine the structure of the CD11 b I domain and to, evaluate the structural effects of divalent ion binding to this protein., RESULTS: We have determined the X-ray structure of a new crystal form of, the CD11 b I domain in the absence of added metal ions by multiple, isomorphous replacement (MIR). Metal ions were easily introduced into this, crystal form allowing the straight-forward assessment of the structural, effects of divalent cation binding at the metal ion dependent adhesion, site (MIDAS). The equilibrium binding constants for these ions were, determined by titration calorimetry. The overall protein conformation and, metal-ion coordination of the I domain is the same as that observed for, all previously reported CD11 a I-domain structures and a CD11 b I-domain, complex with Mn2+. These structures define a majority conformation., CONCLUSIONS: Addition of the cations Mg2+, Mn2+ and Cd2+ to the metal-free, I domain does not induce conformational changes in the crystalline, environment. Moreover, we find that Ca2+ binds poorly to the I domain, which serves to explain its failure to support adhesion. We show that the, active conformation proposed by Lee et al, is likely to be a construct, artifact and we propose that the currently available data do not support a, dramatic structural transition for the I domain during counter-receptor, binding.
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<StructureSection load='1idn' size='340' side='right'caption='[[1idn]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1idn]] is a 2 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=1IDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDN 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]] 2.7&#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=ACE:ACETYL+GROUP'>ACE</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=1idn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idn OCA], [https://pdbe.org/1idn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idn RCSB], [https://www.ebi.ac.uk/pdbsum/1idn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idn 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/1idn_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=1idn 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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1IDN 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 ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDN 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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Cation binding to the integrin CD11b I domain and activation model assessment., Baldwin ET, Sarver RW, Bryant GL Jr, Curry KA, Fairbanks MB, Finzel BC, Garlick RL, Heinrikson RL, Horton NC, Kelley LL, Mildner AM, Moon JB, Mott JE, Mutchler VT, Tomich CS, Watenpaugh KD, Wiley VH, Structure. 1998 Jul 15;6(7):923-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9687375 9687375]
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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: Baldwin, E.T.]]
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[[Category: Baldwin ET]]
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[[Category: ACE]]
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[[Category: cell adhesion]]
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[[Category: i domain]]
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[[Category: integrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:28:56 2007''
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Current revision

MAC-1 I DOMAIN METAL FREE

PDB ID 1idn

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