1mq9

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[[Image:1mq9.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact==
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|PDB= 1mq9 |SIZE=350|CAPTION= <scene name='initialview01'>1mq9</scene>, resolution 2.00&Aring;
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<StructureSection load='1mq9' size='340' side='right'caption='[[1mq9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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<table><tr><td colspan='2'>[[1mq9]] 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=1MQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQ9 FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE= LFA-1 (AlphaLbeta2) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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|DOMAIN=
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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=1mq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq9 OCA], [https://pdbe.org/1mq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mq9 RCSB], [https://www.ebi.ac.uk/pdbsum/1mq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq9 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mq8|1MQ8]], [[1mqa|1MQA]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq9 OCA], [http://www.ebi.ac.uk/pdbsum/1mq9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mq9 RCSB]</span>
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== Function ==
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}}
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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/mq/1mq9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1mq9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the I domain of integrin alpha L beta 2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the alpha L I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligand binding. Pulling down on the C-terminal alpha 7 helix with introduced disulfide bonds ratchets the beta 6-alpha 7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in affinity.
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'''Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact'''
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Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation.,Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA Cell. 2003 Jan 10;112(1):99-111. PMID:12526797<ref>PMID:12526797</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mq9" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of the I domain of integrin alpha L beta 2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the alpha L I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligand binding. Pulling down on the C-terminal alpha 7 helix with introduced disulfide bonds ratchets the beta 6-alpha 7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in affinity.
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*[[Integrin 3D structures|Integrin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1MQ9 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=1MQ9 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation., Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA, Cell. 2003 Jan 10;112(1):99-111. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12526797 12526797]
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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: Dong, Y.]]
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[[Category: Dong Y]]
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[[Category: Joachimiak, A.]]
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[[Category: Joachimiak A]]
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[[Category: Jun, C D.]]
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[[Category: Jun C-D]]
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[[Category: Liu, J H.]]
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[[Category: Liu J-H]]
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[[Category: McCormack, A.]]
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[[Category: McCormack A]]
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[[Category: Shimaoka, M.]]
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[[Category: Shimaoka M]]
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[[Category: Springer, T A.]]
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[[Category: Springer TA]]
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[[Category: Takagi, J.]]
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[[Category: Takagi J]]
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[[Category: Wang, J H.]]
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[[Category: Wang J-H]]
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[[Category: Xiao, T.]]
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[[Category: Xiao T]]
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[[Category: Yang, Y.]]
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[[Category: Yang Y]]
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[[Category: Zhang, R.]]
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[[Category: Zhang R]]
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[[Category: designed disulfide bridge]]
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[[Category: metal mediated protein interface]]
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[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:40 2008''
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Current revision

Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact

PDB ID 1mq9

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