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| [[Image:1zon.gif|left|200px]]<br /><applet load="1zon" size="350" color="white" frame="true" align="right" spinBox="true"
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| caption="1zon, resolution 2.0Å" />
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| '''CD11A I-DOMAIN WITHOUT BOUND CATION'''<br />
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| ==Overview== | | ==CD11A I-DOMAIN WITHOUT BOUND CATION== |
| 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.
| | <StructureSection load='1zon' size='340' side='right'caption='[[1zon]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == |
| | <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> |
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| | <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> |
| | </table> |
| | == Function == |
| | [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. |
| | == 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/zo/1zon_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=1zon ConSurf]. |
| | <div style="clear:both"></div> |
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| ==About this Structure== | | ==See Also== |
| 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZON OCA].
| | *[[Integrin 3D structures|Integrin 3D structures]] |
| | | __TOC__ |
| ==Reference==
| | </StructureSection> |
| 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]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Leahy, D J.]] | | [[Category: Leahy DJ]] |
| [[Category: Qu, A.]] | | [[Category: Qu A]] |
| [[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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:41 2008''
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