1kno

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(New page: 200px<br /> <applet load="1kno" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kno, resolution 3.2&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1kno.gif|left|200px]]<br />
 
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<applet load="1kno" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kno, resolution 3.2&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES==
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The x-ray structure of the complex of a catalytic antibody Fab fragment, with a phosphonate transition-state analog has been determined. The, antibody (CNJ206) catalyzes the hydrolysis of p-nitrophenyl esters with, significant rate enhancement and substrate specificity. Comparison of this, structure with that of the uncomplexed Fab fragment suggests, hapten-induced conformational changes: the shape of the combining site, changes from a shallow groove in the uncomplexed Fab to a deep pocket, where the hapten is buried. Three hydrogen-bond donors appear to stabilize, the charged phosphonate group of the hapten: two NH groups of the heavy, (H) chain complementarity-determining region 3 (H3 CDR) polypeptide chain, and the side-chain of histidine-H35 in the H chain (His-H35) in the H1, CDR. The combining site shows striking structural similarities to that of, antibody 17E8, which also has esterase activity. Both catalytic antibody, ("abzyme") structures suggest that oxyanion stabilization plays a, significant role in their rate acceleration. Additional catalytic groups, that improve efficiency are not necessarily induced by the eliciting, hapten; these groups may occur because of the variability in the combining, sites of different monoclonal antibodies that bind to the same hapten.
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<StructureSection load='1kno' size='340' side='right'caption='[[1kno]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kno]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KNO FirstGlance]. <br>
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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]] 3.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNP:METHYL-PHOSPHONIC+ACID+MONO-(4-NITRO-PHENYL)+ESTER'>PNP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1kno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kno OCA], [https://pdbe.org/1kno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kno RCSB], [https://www.ebi.ac.uk/pdbsum/1kno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kno ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
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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/kn/1kno_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kno 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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The x-ray structure of the complex of a catalytic antibody Fab fragment with a phosphonate transition-state analog has been determined. The antibody (CNJ206) catalyzes the hydrolysis of p-nitrophenyl esters with significant rate enhancement and substrate specificity. Comparison of this structure with that of the uncomplexed Fab fragment suggests hapten-induced conformational changes: the shape of the combining site changes from a shallow groove in the uncomplexed Fab to a deep pocket where the hapten is buried. Three hydrogen-bond donors appear to stabilize the charged phosphonate group of the hapten: two NH groups of the heavy (H) chain complementarity-determining region 3 (H3 CDR) polypeptide chain and the side-chain of histidine-H35 in the H chain (His-H35) in the H1 CDR. The combining site shows striking structural similarities to that of antibody 17E8, which also has esterase activity. Both catalytic antibody ("abzyme") structures suggest that oxyanion stabilization plays a significant role in their rate acceleration. Additional catalytic groups that improve efficiency are not necessarily induced by the eliciting hapten; these groups may occur because of the variability in the combining sites of different monoclonal antibodies that bind to the same hapten.
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==About this Structure==
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Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodies.,Charbonnier JB, Carpenter E, Gigant B, Golinelli-Pimpaneau B, Eshhar Z, Green BS, Knossow M Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11721-5. PMID:8524836<ref>PMID:8524836</ref>
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1KNO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and PNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KNO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodies., Charbonnier JB, Carpenter E, Gigant B, Golinelli-Pimpaneau B, Eshhar Z, Green BS, Knossow M, Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11721-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8524836 8524836]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1kno" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Charbonnier, J.B.]]
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[[Category: Gigant, B.]]
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[[Category: Knossow, M.]]
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[[Category: PNP]]
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[[Category: ZN]]
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[[Category: catalytic antibody]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:35:14 2007''
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==See Also==
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Charbonnier J-B]]
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[[Category: Gigant B]]
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[[Category: Knossow M]]

Current revision

CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES

PDB ID 1kno

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