1f3d
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(New page: 200px<br /> <applet load="1f3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3d, resolution 1.87Å" /> '''CATALYTIC ANTIBODY ...)
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Revision as of 07:22, 18 November 2007
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CATALYTIC ANTIBODY 4B2 IN COMPLEX WITH ITS AMIDINIUM HAPTEN.
Overview
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
1F3D is a Protein complex structure of sequences from Mus musculus with SO4 and TPM as ligands. Full crystallographic information is available from OCA.
Reference
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
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