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1eap

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(New page: 200px<br /> <applet load="1eap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eap, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1eap.gif|left|200px]]<br />
 
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<applet load="1eap" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eap, resolution 2.4&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE==
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The three-dimensional structure of an unusually active hydrolytic antibody, with a phosphonate transition state analog (hapten) bound to the active, site has been solved to 2.5 A resolution. The antibody (17E8) catalyzes, the hydrolysis of norleucine and methionine phenyl esters and is selective, for amino acid esters that have the natural alpha-carbon L configuration., A plot of the pH-dependence of the antibody-catalyzed reaction is, bell-shaped with an activity maximum at pH 9.5; experiments on mechanism, lend support to the formation of a covalent acyl-antibody intermediate., The structural and kinetic data are complementary and support a hydrolytic, mechanism for the antibody that is remarkably similar to that of the, serine proteases. The antibody active site contains a Ser-His dyad, structure proximal to the phosphorous atom of the bound hapten that, resembles two of the three components of the Ser-His-Asp catalytic triad, of serine proteases. The antibody active site also contains a Lys residue, to stabilize oxyanion formation, and a hydrophobic binding pocket for, specific substrate recognition of norleucine and methionine side chains., The structure identifies active site residues that mediate catalysis and, suggests specific mutations that may improve the catalytic efficiency of, the antibody. This high resolution structure of a catalytic, antibody-hapten complex shows that antibodies can converge on active site, structures that have arisen through natural enzyme evolution.
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<StructureSection load='1eap' size='340' side='right'caption='[[1eap]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eap]] is a 2 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=1EAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAP 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]] 2.4&#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=HEP:PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE'>HEP</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=1eap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eap OCA], [https://pdbe.org/1eap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eap RCSB], [https://www.ebi.ac.uk/pdbsum/1eap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eap ProSAT]</span></td></tr>
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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/ea/1eap_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=1eap ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with HEP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EAP OCA].
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of a catalytic antibody with a serine protease active site., Zhou GW, Guo J, Huang W, Fletterick RJ, Scanlan TS, Science. 1994 Aug 19;265(5175):1059-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8066444 8066444]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Fletterick RJ]]
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[[Category: Fletterick, R.J.]]
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[[Category: Guo J]]
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[[Category: Guo, J.]]
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[[Category: Huang W]]
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[[Category: Huang, W.]]
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[[Category: Scanlan TS]]
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[[Category: Scanlan, T.S.]]
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[[Category: Zhou GW]]
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[[Category: Zhou, G.W.]]
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[[Category: HEP]]
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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 09:29:08 2007''
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Current revision

CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE

PDB ID 1eap

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