1kn2: Difference between revisions

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{{Seed}}
[[Image:1kn2.png|left|200px]]


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==CATALYTIC ANTIBODY D2.3 COMPLEX==
The line below this paragraph, containing "STRUCTURE_1kn2", creates the "Structure Box" on the page.
<StructureSection load='1kn2' size='340' side='right'caption='[[1kn2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1kn2]] 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=1KN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KN2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=PNE:PARA-NITROPHENYL+PHOSPHONOBUTANOYL+L-ALANINE'>PNE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1kn2|  PDB=1kn2  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn2 OCA], [https://pdbe.org/1kn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kn2 RCSB], [https://www.ebi.ac.uk/pdbsum/1kn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q58EU8_MOUSE Q58EU8_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/kn/1kn2_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=1kn2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of catalytic antibody D2.3 Fab with the two enantiomers, 7D and 7L, which represent transition state analogues for the hydrolysis of the corresponding esters, 6D and 6L, were determined to better understand remarkable reactivity differences: the L-ester displayed significantly tighter binding (K(M)) and increased catalytic activity (k(cat)) with D2.3, even though the chiral center is 7 bonds distant from the reaction center. Surprisingly, the electron densities of the liganded phosphonates, 7D and 7L, within the D2.3 binding/reaction site were essentially identical, highlighting the subtle influences of protein interactions on chemical behavior.


===CATALYTIC ANTIBODY D2.3 COMPLEX===
Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody.,D'Souza LJ, Gigant B, Knossow M, Green BS J Am Chem Soc. 2002 Mar 13;124(10):2114-5. PMID:11878955<ref>PMID:11878955</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kn2" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11878955}}, adds the Publication Abstract to the page
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11878955 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_11878955}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1KN2 is a 2 chains structure of sequences 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=1KN2 OCA].
 
==Reference==
<ref group="xtra">PMID:11878955</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Gigant, B.]]
[[Category: Gigant B]]
[[Category: Knossow, M.]]
[[Category: Knossow M]]
[[Category: Abzyme]]
[[Category: Immune system]]
[[Category: Transition state analog]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:31:34 2009''

Latest revision as of 10:20, 9 October 2024

CATALYTIC ANTIBODY D2.3 COMPLEXCATALYTIC ANTIBODY D2.3 COMPLEX

Structural highlights

1kn2 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q58EU8_MOUSE

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 PubMed

The crystal structures of catalytic antibody D2.3 Fab with the two enantiomers, 7D and 7L, which represent transition state analogues for the hydrolysis of the corresponding esters, 6D and 6L, were determined to better understand remarkable reactivity differences: the L-ester displayed significantly tighter binding (K(M)) and increased catalytic activity (k(cat)) with D2.3, even though the chiral center is 7 bonds distant from the reaction center. Surprisingly, the electron densities of the liganded phosphonates, 7D and 7L, within the D2.3 binding/reaction site were essentially identical, highlighting the subtle influences of protein interactions on chemical behavior.

Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody.,D'Souza LJ, Gigant B, Knossow M, Green BS J Am Chem Soc. 2002 Mar 13;124(10):2114-5. PMID:11878955[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. D'Souza LJ, Gigant B, Knossow M, Green BS. Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody. J Am Chem Soc. 2002 Mar 13;124(10):2114-5. PMID:11878955

1kn2, resolution 1.90Å

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