1f3d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==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.
+
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==
==About this Structure==
Line 25: Line 25:
[[Category: haptenic charge]]
[[Category: haptenic charge]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:45:33 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:22 2008''

Revision as of 10:34, 21 February 2008


1f3d, resolution 1.87Å

Drag the structure with the mouse to rotate

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 and 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

Page seeded by OCA on Thu Feb 21 12:34:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools