1zon

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(New page: 200px<br /> <applet load="1zon" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zon, resolution 2.0&Aring;" /> '''CD11A I-DOMAIN WITHO...)
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[[Image:1zon.gif|left|200px]]<br />
 
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<applet load="1zon" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zon, resolution 2.0&Aring;" />
 
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'''CD11A I-DOMAIN WITHOUT BOUND CATION'''<br />
 
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==Overview==
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==CD11A I-DOMAIN WITHOUT BOUND CATION==
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BACKGROUND: The integrin family of cell-surface receptors mediates a wide, variety of cell-cell and cell-extracellular matrix interactions., Integrin-ligand interactions are invariably dependent on the presence of, divalent cations, and a subset of integrins contain a approximately 200, amino acid inserted (I) domain that is important for ligand binding, activity and contains a single divalent cation binding site. Many, integrins are believed to respond to stimuli by undergoing a, conformational change that increases their affinity for ligand, and there, is a clear difference between two crystal structures of the CD11b I domain, with different divalent cations (magnesium and manganese) bound. In, addition to the different bound cation, a 'ligand mimetic' crystal lattice, interaction in the CD11b I domain structure with bound magnesium has led, to the interpretation that the different CD11b I domain structures, represent different affinity states of I domains. The influence of the, bound cation on I domain structure and function remains incompletely, understood, however. The crystal structure of the CD11a I domain bound to, manganese is known. We therefore set out to determine whether this, structure changes when the metal ion is altered or removed. RESULTS: We, report here the crystal structures of the CD11a I domain determined in the, absence of bound metal ion and with bound magnesium ion. No major, structural rearrangements are observed in the metal-binding site of the, CD11a I domain in the absence or presence of bound manganese ion. The, structures of the CD11a I domain with magnesium or manganese bound are, extremely similar. CONCLUSIONS: The conformation of the CD11a I domain is, not altered by changes in metal ion binding. The cation-dependence of, ligand binding thus indicates that the metal ion is either involved in, direct interaction with ligand or required to promote a favorable, quaternary arrangement of the integrin.
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<StructureSection load='1zon' size='340' side='right'caption='[[1zon]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zon]] 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=1ZON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZON 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&#8491;</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=1zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zon OCA], [https://pdbe.org/1zon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zon RCSB], [https://www.ebi.ac.uk/pdbsum/1zon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zon ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ITAL_HUMAN ITAL_HUMAN] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.
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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/zo/1zon_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=1zon 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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1ZON 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=1ZON 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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The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin., Qu A, Leahy DJ, Structure. 1996 Aug 15;4(8):931-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805579 8805579]
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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: Leahy, D.J.]]
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[[Category: Leahy DJ]]
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[[Category: Qu, A.]]
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[[Category: Qu A]]
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[[Category: cell adhesion]]
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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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[[Category: signal]]
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[[Category: transmembrane]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:37:53 2007''
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Current revision

CD11A I-DOMAIN WITHOUT BOUND CATION

PDB ID 1zon

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