1kn2: Difference between revisions

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New page: left|200px<br /> <applet load="1kn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kn2, resolution 1.90Å" /> '''CATALYTIC ANTIBODY ...
 
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[[Image:1kn2.gif|left|200px]]<br />
[[Image:1kn2.gif|left|200px]]<br /><applet load="1kn2" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1kn2" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1kn2, resolution 1.90&Aring;" />
caption="1kn2, resolution 1.90&Aring;" />
'''CATALYTIC ANTIBODY D2.3 COMPLEX'''<br />
'''CATALYTIC ANTIBODY D2.3 COMPLEX'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1KN2 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 ZN and PNE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KN2 OCA].  
1KN2 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 <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PNE:'>PNE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN2 OCA].  


==Reference==
==Reference==
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[[Category: transition state analog]]
[[Category: transition state analog]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:51 2008''

Revision as of 14:35, 21 February 2008

File:1kn2.gif


1kn2, resolution 1.90Å

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CATALYTIC ANTIBODY D2.3 COMPLEX

OverviewOverview

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.

About this StructureAbout this Structure

1KN2 is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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