1fn4: Difference between revisions
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[[Image: | ==CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES== | ||
<StructureSection load='1fn4' size='340' side='right' caption='[[1fn4]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1fn4]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FN4 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fn4 RCSB], [http://www.ebi.ac.uk/pdbsum/1fn4 PDBsum]</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/fn/1fn4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Eliopoulos, E.]] | [[Category: Eliopoulos, E.]] | ||
Revision as of 17:13, 28 September 2014
CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIESCRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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