1fn4: Difference between revisions

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-[[Image:1fn4.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1fn4", creates the "Structure Box" on the page.
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-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.
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-{{STRUCTURE_1fn4|  PDB=1fn4  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES'''
+==CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES==
+<StructureSection load='1fn4' size='340' side='right'caption='[[1fn4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fn4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FN4 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]] 2.8&#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=1fn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn4 OCA], [https://pdbe.org/1fn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1fn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fn4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IGG2A_RAT IGG2A_RAT]
+== 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/fn/1fn4_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=1fn4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the Fab fragment of the rat monoclonal antibody 198, with protective activity for the main immunogenic region of the human muscle acetylcholine receptor against the destructive action of myasthenic antibodies, has been determined and refined to 2.8 A resolution by X-ray crystallographic methods. The mouse anti-lysozyme Fab D1.3 was used as a search model in molecular replacement with the AMORE software. The complementarity determining regions (CDR)-L2, CDR-H1 and CDR-H2 belong to canonical groups. Loops CDR-L3, CDR-H2 and CDR-H3, which seem to make a major contribution to binding, were analyzed and residues of potential importance for antigen-binding are examined. The antigen-binding site was found to be a long crescent-shaped crevice. The structure should serve as a model in the rational design of very high affinity humanized mutants of Fab198, appropriate for therapeutic approaches in the model autoimmune disease myasthenia gravis.
-==Overview==
+Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies.,Poulas K, Eliopoulos E, Vatzaki E, Navaza J, Kontou M, Oikonomakos N, Acharya KR, Tzartos SJ Eur J Biochem. 2001 Jul;268(13):3685-93. PMID:11432734<ref>PMID:11432734</ref>
-The crystal structure of the Fab fragment of the rat monoclonal antibody 198, with protective activity for the main immunogenic region of the human muscle acetylcholine receptor against the destructive action of myasthenic antibodies, has been determined and refined to 2.8 A resolution by X-ray crystallographic methods. The mouse anti-lysozyme Fab D1.3 was used as a search model in molecular replacement with the AMORE software. The complementarity determining regions (CDR)-L2, CDR-H1 and CDR-H2 belong to canonical groups. Loops CDR-L3, CDR-H2 and CDR-H3, which seem to make a major contribution to binding, were analyzed and residues of potential importance for antigen-binding are examined. The antigen-binding site was found to be a long crescent-shaped crevice. The structure should serve as a model in the rational design of very high affinity humanized mutants of Fab198, appropriate for therapeutic approaches in the model autoimmune disease myasthenia gravis.
-==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=1FN4 OCA].
+</div>
+<div class="pdbe-citations 1fn4" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies., Poulas K, Eliopoulos E, Vatzaki E, Navaza J, Kontou M, Oikonomakos N, Acharya KR, Tzartos SJ, Eur J Biochem. 2001 Jul;268(13):3685-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11432734 11432734]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-[[Category: Eliopoulos, E.]]
+== References ==
-[[Category: Kontou, M.]]
+<references/>
-[[Category: Navaza, J.]]
+__TOC__
-[[Category: Poulas, K.]]
+</StructureSection>
-[[Category: Vatzaki, E.]]
+[[Category: Large Structures]]
-[[Category: Fab198]]
+[[Category: Rattus norvegicus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:31:31 2008''
+[[Category: Eliopoulos E]]
+[[Category: Kontou M]]
+[[Category: Navaza J]]
+[[Category: Poulas K]]
+[[Category: Vatzaki E]]