3eob: Difference between revisions

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-{{Seed}}
-[[Image:3eob.jpg|left|200px]]
-<!--
+==Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II==
-The line below this paragraph, containing "STRUCTURE_3eob", creates the "Structure Box" on the page.
+<StructureSection load='3eob' size='340' side='right'caption='[[3eob]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3eob]] is a 6 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=3EOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EOB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</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>
-{{STRUCTURE_3eob|  PDB=3eob  |  SCENE=  }}
+<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>
+</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/eo/3eob_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3eob ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3eob" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19258452}}, adds the Publication Abstract to the page
+*[[Integrin 3D structures|Integrin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19258452 is the PubMed ID number.
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_19258452}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-EOB is a 6 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=3EOB OCA].
-==Reference==
-<ref group="xtra">PMID:19258452</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Ding, J.]]
+[[Category: Large Structures]]
-[[Category: Li, S.]]
+[[Category: Ding J]]
-[[Category: Alternative splicing]]
+[[Category: Li S]]
-[[Category: Antibody]]
-[[Category: Calcium]]
-[[Category: Cd11a]]
-[[Category: Cell adhesion]]
-[[Category: Efalizumab]]
-[[Category: Fab]]
-[[Category: Glycoprotein]]
-[[Category: I domain]]
-[[Category: Immune system/cell adhesion complex]]
-[[Category: Integrin]]
-[[Category: Lfa-1]]
-[[Category: Magnesium]]
-[[Category: Membrane]]
-[[Category: Polymorphism]]
-[[Category: Receptor]]
-[[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 15 10:27:55 2009''