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1c5b

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[[Image:1c5b.gif|left|200px]]
 
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==DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM==
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The line below this paragraph, containing "STRUCTURE_1c5b", creates the "Structure Box" on the page.
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<StructureSection load='1c5b' size='340' side='right'caption='[[1c5b]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1c5b]] is a 2 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=1C5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C5B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=1c5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5b OCA], [https://pdbe.org/1c5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c5b RCSB], [https://www.ebi.ac.uk/pdbsum/1c5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c5b ProSAT]</span></td></tr>
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{{STRUCTURE_1c5b| PDB=1c5b | SCENE= }}
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</table>
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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/c5/1c5b_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=1c5b 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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Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of 3-carboxybenzisoxazoles. The crystal structure of chimeric Fab 21D8 with and without hapten at 1.61 A and 2.10 A, respectively, together with computational analysis, shows how a melange of polar and non-polar sites are exploited to achieve both substrate binding and acceleration of a reaction normally facilitated by purely aprotic dipolar media. The striking similarity of the decarboxylase and a series of unrelated esterase antibodies also highlights the chemical versatility of structurally conserved anion binding sites and the relatively subtle changes involved in fine-tuning the immunoglobulin pocket for recognition of different ligands and catalysis of different reactions.
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'''DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM'''
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Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8.,Hotta K, Lange H, Tantillo DJ, Houk KN, Hilvert D, Wilson IA J Mol Biol. 2000 Oct 6;302(5):1213-25. PMID:11183784<ref>PMID:11183784</ref>
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==Overview==
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Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of 3-carboxybenzisoxazoles. The crystal structure of chimeric Fab 21D8 with and without hapten at 1.61 A and 2.10 A, respectively, together with computational analysis, shows how a melange of polar and non-polar sites are exploited to achieve both substrate binding and acceleration of a reaction normally facilitated by purely aprotic dipolar media. The striking similarity of the decarboxylase and a series of unrelated esterase antibodies also highlights the chemical versatility of structurally conserved anion binding sites and the relatively subtle changes involved in fine-tuning the immunoglobulin pocket for recognition of different ligands and catalysis of different reactions.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5B OCA].
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</div>
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<div class="pdbe-citations 1c5b" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8., Hotta K, Lange H, Tantillo DJ, Houk KN, Hilvert D, Wilson IA, J Mol Biol. 2000 Oct 6;302(5):1213-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11183784 11183784]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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[[Category: Hotta, K.]]
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== References ==
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[[Category: Wilson, I A.]]
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<references/>
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[[Category: Catalytic antibody]]
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__TOC__
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[[Category: Chimeric fab]]
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</StructureSection>
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[[Category: Decarboxylase]]
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[[Category: Homo sapiens]]
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[[Category: Immunoglobulin]]
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[[Category: Large Structures]]
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[[Category: Unliganded]]
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[[Category: Mus musculus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:20:46 2008''
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[[Category: Hotta K]]
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[[Category: Wilson IA]]

Current revision

DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM

PDB ID 1c5b

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