2p28

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{{Seed}}
 
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[[Image:2p28.png|left|200px]]
 
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==Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit==
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The line below this paragraph, containing "STRUCTURE_2p28", creates the "Structure Box" on the page.
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<StructureSection load='2p28' size='340' side='right'caption='[[2p28]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2p28]] 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=2P28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P28 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_2p28| PDB=2p28 | SCENE= }}
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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=2p28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p28 OCA], [https://pdbe.org/2p28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p28 RCSB], [https://www.ebi.ac.uk/pdbsum/2p28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p28 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN] Defects in ITGB2 are the cause of leukocyte adhesion deficiency type 1 (LAD1) [MIM:[https://omim.org/entry/116920 116920]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.<ref>PMID:7509236</ref> <ref>PMID:1346613</ref> <ref>PMID:1968911</ref> <ref>PMID:1694220</ref> <ref>PMID:1590804</ref> <ref>PMID:1352501</ref> <ref>PMID:1347532</ref> <ref>PMID:7686755</ref> <ref>PMID:9884339</ref> <ref>PMID:20529581</ref> <ref>PMID:20549317</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>
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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/p2/2p28_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=2p28 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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Integrins mediate cell adhesion in response to activation signals that trigger conformational changes within their ectodomain. It is thought that a compact bent conformation of the molecule represents its physiological low affinity state and extended conformations its active state. We have determined the structure of two integrin fragments of the beta2 subunit. The first structure, consisting of the plexin-semaphorin-integrin domain, hybrid, integrin-epidermal growth factor 1 (I-EGF1), and I-EGF2 domains (PHE2), showed an L-shaped conformation with the bend located between the I-EGF1 and I-EGF2 domains. The second structure, which includes, in addition, the I-EGF3 domain, showed an extended conformation. The major reorientation of I-EGF2 with respect to the other domains in the two structures is accompanied by a change of torsion angle of the disulfide bond between Cys(461)-Cys(492) by 180 degrees and the conversion of a short alpha-helix (residues Ser(468)-Cys(475)) into a flexible coil. Based on the PHE2 structure, we introduced a disulfide bond between the plexin-semaphorin-integrin domain and I-EGF2 domains in the beta2 subunit. The resultant alphaLbeta2 integrin (leukocyte function-associated antigen-1) variant was locked in a bent state and could not be detected with the monoclonal antibody KIM127 in Mg(2+)/EGTA. However, it retained the binding activity to ICAM-1. These results provide a structural hypothesis for our understanding of the transition between the resting and active states of leukocyte function-associated antigen-1.
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===Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit===
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A structural hypothesis for the transition between bent and extended conformations of the leukocyte beta2 integrins.,Shi M, Foo SY, Tan SM, Mitchell EP, Law SK, Lescar J J Biol Chem. 2007 Oct 12;282(41):30198-206. Epub 2007 Aug 1. PMID:17673459<ref>PMID:17673459</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 2p28" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17673459}}, adds the Publication Abstract to the page
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*[[Integrin 3D structures|Integrin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17673459 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17673459}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2P28 is a 2 chains structure of sequences 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=2P28 OCA].
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==Reference==
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<ref group="xtra">PMID:17673459</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Foo, S Y.]]
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[[Category: Large Structures]]
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[[Category: Law, S K.A.]]
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[[Category: Foo SY]]
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[[Category: Lescar, J.]]
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[[Category: Law SKA]]
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[[Category: Mitchell, E P.]]
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[[Category: Lescar J]]
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[[Category: Shi, M.]]
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[[Category: Mitchell EP]]
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[[Category: Tan, S M.]]
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[[Category: Shi M]]
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[[Category: Cell adhesion]]
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[[Category: Tan SM]]
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[[Category: Crystal structure]]
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[[Category: Hybrid domain]]
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[[Category: I-egf domain]]
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[[Category: Integrin beta2 subunit]]
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[[Category: Psi domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:42:33 2009''
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Current revision

Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit

PDB ID 2p28

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