1lo4: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lo4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LO4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1lo4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LO4 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l00|1l00]], [[1l02|1l02]], [[1l03|1l03]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l00|1l00]], [[1l02|1l02]], [[1l03|1l03]]</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=1lo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lo4 RCSB], [http://www.ebi.ac.uk/pdbsum/1lo4 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lo4 RCSB], [http://www.ebi.ac.uk/pdbsum/1lo4 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Baumann, U | [[Category: Baumann, U]] | ||
[[Category: Hugot, M | [[Category: Hugot, M]] | ||
[[Category: Reymond, J L | [[Category: Reymond, J L]] | ||
[[Category: Catalytic antibody]] | [[Category: Catalytic antibody]] | ||
[[Category: Fab]] | [[Category: Fab]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Retro-deils-alderase]] | [[Category: Retro-deils-alderase]] | ||
Revision as of 18:35, 5 January 2015
Retro-Diels-Alderase Catalytic antibody 9D9Retro-Diels-Alderase Catalytic antibody 9D9
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 nitroxyl synthase catalytic antibodies 10F11, 9D9, and 27C5 catalyze the release of nitroxyl from a bicyclic pro-drug by accelerating a retro-Diels-Alder reaction. The Fabs (antigen-binding fragments) of these three catalytic antibodies were cloned and sequenced. Fab 9D9 was crystallized in the apo-form and in complex with one transition state analogue of the reaction. Crystal structures of Fab 10F11 in complex with ligands mimicking substrate, transition state, and product have been determined at resolutions ranging from 1.8 to 2.3 A. Antibodies 9D9 and 10F11 show increased shape complementarity (as quantified by the program sc) to the hapten and to a modeled transition state as compared with substrate and product. The shape complementarity is mediated to a large extent by an aromatic residue (tyrosine or tryptophan) at the bottom of the hydrophobic active pocket, which undergoes pi-stacking interactions with the aromatic rings of the ligands. Another factor contributing to the different reactivity of the regioisomers probably arises because of hydrogen-bonding interactions between the nitroxyl bridge and the backbone amide of PheH101 and possibly a conserved water molecule. A structural basis for the activity of retro-Diels-Alder catalytic antibodies: evidence for a catalytic aromatic residue.,Hugot M, Bensel N, Vogel M, Reymond MT, Stadler B, Reymond JL, Baumann U Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9674-8. Epub 2002 Jul 1. PMID:12093912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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