1f3d: Difference between revisions

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[[Image:1f3d.jpg|left|200px]]
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{{STRUCTURE_1f3d|  PDB=1f3d  |  SCENE=  }}
'''CATALYTIC ANTIBODY 4B2 IN COMPLEX WITH ITS AMIDINIUM HAPTEN.'''


==CATALYTIC ANTIBODY 4B2 IN COMPLEX WITH ITS AMIDINIUM HAPTEN.==
<StructureSection load='1f3d' size='340' side='right'caption='[[1f3d]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f3d]] is a 4 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=1F3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3D 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]] 1.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPM:2-(4-AMINOBENZYLAMINO)-3,4,5,6-TETRAHYDROPYRIDINIUM'>TPM</scene></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=1f3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3d OCA], [https://pdbe.org/1f3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3d RCSB], [https://www.ebi.ac.uk/pdbsum/1f3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2NHM3_MOUSE A2NHM3_MOUSE]
== 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/f3/1f3d_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=1f3d ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the complex of a catalytic antibody with its cationic hapten at 1.9-A resolution demonstrates that the hapten amidinium group is stabilized through an ionic pair interaction with the carboxylate of a combining-site residue. The location of this carboxylate allows it to act as a general base in an allylic rearrangement. When compared with structures of other antibody complexes in which the positive moiety of the hapten is stabilized mostly by cation-pi interactions, this structure shows that the amidinium moiety is a useful candidate to elicit a carboxylate in an antibody combining site at a predetermined location with respect to the hapten. More generally, this structure highlights the advantage of a bidentate hapten for the programmed positioning of a chemically reactive residue in an antibody through charge complementarity to the hapten.


==Overview==
Structural evidence for a programmed general base in the active site of a catalytic antibody.,Golinelli-Pimpaneau B, Goncalves O, Dintinger T, Blanchard D, Knossow M, Tellier C Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9892-5. PMID:10963661<ref>PMID:10963661</ref>
The crystal structure of the complex of a catalytic antibody with its cationic hapten at 1.9-A resolution demonstrates that the hapten amidinium group is stabilized through an ionic pair interaction with the carboxylate of a combining-site residue. The location of this carboxylate allows it to act as a general base in an allylic rearrangement. When compared with structures of other antibody complexes in which the positive moiety of the hapten is stabilized mostly by cation-pi interactions, this structure shows that the amidinium moiety is a useful candidate to elicit a carboxylate in an antibody combining site at a predetermined location with respect to the hapten. More generally, this structure highlights the advantage of a bidentate hapten for the programmed positioning of a chemically reactive residue in an antibody through charge complementarity to the hapten.


==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=1F3D OCA].
</div>
<div class="pdbe-citations 1f3d" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural evidence for a programmed general base in the active site of a catalytic antibody., Golinelli-Pimpaneau B, Goncalves O, Dintinger T, Blanchard D, Knossow M, Tellier C, Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9892-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10963661 10963661]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
[[Category: Blanchard, D.]]
== References ==
[[Category: Dintinger, T.]]
<references/>
[[Category: Golinelli-Pimpaneau, B.]]
__TOC__
[[Category: Goncalves, O.]]
</StructureSection>
[[Category: Knossow, M.]]
[[Category: Large Structures]]
[[Category: Tellier, C.]]
[[Category: Mus musculus]]
[[Category: Amidinium]]
[[Category: Blanchard D]]
[[Category: Catalytic antibody]]
[[Category: Dintinger T]]
[[Category: Haptenic charge]]
[[Category: Golinelli-Pimpaneau B]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:50:42 2008''
[[Category: Goncalves O]]
[[Category: Knossow M]]
[[Category: Tellier C]]
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