This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lo4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1lo4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lo4, resolution 2.40&Aring;" /> '''Retro-Diels-Alderas...)
Current revision (08:25, 10 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lo4.gif|left|200px]]<br />
 
-
<applet load="1lo4" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1lo4, resolution 2.40&Aring;" />
 
-
'''Retro-Diels-Alderase Catalytic antibody 9D9'''<br />
 
-
==Overview==
+
==Retro-Diels-Alderase Catalytic antibody 9D9==
-
The 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.
+
<StructureSection load='1lo4' size='340' side='right'caption='[[1lo4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1lo4]] 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=1LO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LO4 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]] 2.4&#8491;</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=1lo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo4 OCA], [https://pdbe.org/1lo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lo4 RCSB], [https://www.ebi.ac.uk/pdbsum/1lo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lo4 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q65ZC0_MOUSE Q65ZC0_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/lo/1lo4_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lo4 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1LO4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LO4 OCA].
+
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12093912 12093912]
+
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Baumann U]]
-
[[Category: Baumann, U.]]
+
[[Category: Hugot M]]
-
[[Category: Hugot, M.]]
+
[[Category: Reymond JL]]
-
[[Category: Reymond, J.L.]]
+
-
[[Category: catalytic antibody]]
+
-
[[Category: fab]]
+
-
[[Category: retro-deils-alderase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:36:01 2007''
+

Current revision

Retro-Diels-Alderase Catalytic antibody 9D9

PDB ID 1lo4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools