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3eob

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[[Image:3eob.png|left|200px]]
 
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{{STRUCTURE_3eob| PDB=3eob | SCENE= }}
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==Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II==
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<StructureSection load='3eob' size='340' side='right'caption='[[3eob]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3eob]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EOB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eo9|3eo9]], [[3eoa|3eoa]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LFA-1 I domain ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eob OCA], [https://pdbe.org/3eob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eob RCSB], [https://www.ebi.ac.uk/pdbsum/3eob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eob 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/eo/3eob_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=3eob 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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Lymphocyte function-associated antigen 1 (LFA-1) plays important roles in immune cell adhesion, trafficking, and activation and is a therapeutic target for the treatment of multiple autoimmune diseases. Efalizumab is one of the most efficacious antibody drugs for treating psoriasis, a very common skin disease, through inhibition of the binding of LFA-1 to the ligand intercellular adhesion molecule 1 (ICAM-1). We report here the crystal structures of the Efalizumab Fab alone and in complex with the LFA-1 alpha(L) I domain, which reveal the molecular mechanism of inhibition of LFA-1 by Efalizumab. The Fab binds with an epitope on the inserted (I) domain that is distinct from the ligand-binding site. Efalizumab binding blocks the binding of LFA-1 to ICAM-1 via steric hindrance between its light chain and ICAM-1 domain 2 and thus inhibits the activities of LFA-1. These results have important implications for the development of improved antibodies and new therapeutic strategies for the treatment of autoimmune diseases.
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===Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II===
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Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance.,Li S, Wang H, Peng B, Zhang M, Zhang D, Hou S, Guo Y, Ding J Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4349-54. Epub 2009 Mar 3. PMID:19258452<ref>PMID:19258452</ref>
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{{ABSTRACT_PUBMED_19258452}}
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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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==About this Structure==
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<div class="pdbe-citations 3eob" style="background-color:#fffaf0;"></div>
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[[3eob]] is a 6 chain structure of [[Monoclonal Antibody]] with 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=3EOB OCA].
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==See Also==
==See Also==
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*[[Monoclonal Antibody|Monoclonal Antibody]]
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*[[Integrin 3D structures|Integrin 3D structures]]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:019258452</ref><references group="xtra"/>
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<references/>
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[[Category: Homo sapiens]]
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__TOC__
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[[Category: Ding, J.]]
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</StructureSection>
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[[Category: Li, S.]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Ding, J]]
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[[Category: Li, S]]
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[[Category: Alternative splicing]]
[[Category: Antibody]]
[[Category: Antibody]]
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[[Category: Calcium]]
[[Category: Cd11a]]
[[Category: Cd11a]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
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[[Category: Magnesium]]
[[Category: Magnesium]]
[[Category: Membrane]]
[[Category: Membrane]]
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[[Category: Polymorphism]]
[[Category: Receptor]]
[[Category: Receptor]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]

Current revision

Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II

PDB ID 3eob

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