1yy8: Difference between revisions

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-[[Image:1yy8.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1yy8", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1yy8|  PDB=1yy8  |  SCENE=  }}
-'''Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225'''
+==Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225==
+<StructureSection load='1yy8' size='340' side='right'caption='[[1yy8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1yy8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YY8 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]] 2&#8491;</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=1yy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yy8 OCA], [https://pdbe.org/1yy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1yy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yy8 ProSAT]</span></td></tr>
+</table>
+== 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/yy/1yy8_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=1yy8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Recent structural studies of epidermal growth factor receptor (EGFR) family extracellular regions have identified an unexpected mechanism for ligand-induced receptor dimerization that has important implications for activation and inhibition of these receptors. Here we describe the 2.8 angstroms resolution X-ray crystal structure of the antigen binding (Fab) fragment from cetuximab (Erbitux), an inhibitory anti-EGFR antibody, in complex with the soluble extracellular region of EGFR (sEGFR). The sEGFR is in the characteristic "autoinhibited" or "tethered" inactive configuration. Cetuximab interacts exclusively with domain III of sEGFR, partially occluding the ligand binding region on this domain and sterically preventing the receptor from adopting the extended conformation required for dimerization. We suggest that both these effects contribute to potent inhibition of EGFR activation.
-==Overview==
+Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.,Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM Cancer Cell. 2005 Apr;7(4):301-11. PMID:15837620<ref>PMID:15837620</ref>
-Recent structural studies of epidermal growth factor receptor (EGFR) family extracellular regions have identified an unexpected mechanism for ligand-induced receptor dimerization that has important implications for activation and inhibition of these receptors. Here we describe the 2.8 angstroms resolution X-ray crystal structure of the antigen binding (Fab) fragment from cetuximab (Erbitux), an inhibitory anti-EGFR antibody, in complex with the soluble extracellular region of EGFR (sEGFR). The sEGFR is in the characteristic "autoinhibited" or "tethered" inactive configuration. Cetuximab interacts exclusively with domain III of sEGFR, partially occluding the ligand binding region on this domain and sterically preventing the receptor from adopting the extended conformation required for dimerization. We suggest that both these effects contribute to potent inhibition of EGFR activation.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY8 OCA].
+</div>
+<div class="pdbe-citations 1yy8" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis for inhibition of the epidermal growth factor receptor by cetuximab., Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM, Cancer Cell. 2005 Apr;7(4):301-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15837620 15837620]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-[[Category: Ferguson, K M.]]
+== References ==
-[[Category: Jeffrey, P D.]]
+<references/>
-[[Category: Kussie, P.]]
+__TOC__
-[[Category: Li, S.]]
+</StructureSection>
-[[Category: Schmitz, K R.]]
+[[Category: Homo sapiens]]
-[[Category: Wiltzius, J J.W.]]
+[[Category: Large Structures]]
-[[Category: Antibody drug]]
+[[Category: Mus musculus]]
-[[Category: Cancer]]
+[[Category: Ferguson KM]]
-[[Category: Fab fragment]]
+[[Category: Jeffrey PD]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:57:04 2008''
+[[Category: Kussie P]]
+[[Category: Li S]]
+[[Category: Schmitz KR]]
+[[Category: Wiltzius JJW]]