1a0q: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1a0q.gif|left|200px]] | [[Image:1a0q.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1a0q", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1a0q| PDB=1a0q | SCENE= }} | |||
}} | |||
'''29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE''' | '''29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE''' | ||
| Line 29: | Line 26: | ||
[[Category: Scanlan, T S.]] | [[Category: Scanlan, T S.]] | ||
[[Category: Stephenson, R C.]] | [[Category: Stephenson, R C.]] | ||
[[Category: | [[Category: Catalytic antibody]] | ||
[[Category: | [[Category: Esterase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:38:26 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:38, 2 May 2008
29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE
OverviewOverview
The crystallographic structure of the Fab fragment of the catalytic antibody, 29G11, complexed with an (S)-norleucine phenyl phosphonate transition state analog was determined at 2.2 A resolution. The antibody catalyzes the hydrolysis of norleucine phenyl ester with (S)-enantioselectivity. The shape and charge complementarity of the binding pocket for the hapten account for the preferential binding of the (S)-enantiomer of the substrate. The structure is compared to that of the more catalytically efficient antibody, 17E8, induced by the same hapten transition state analog. 29G11 has different residues from 17E8 at eight positions in the heavy chain, including four substitutions in the hapten-binding pocket: A33V, S95G, S99R and Y100AN, and four substitutions at positions remote from the catalytic site, I28T, R40K, V65G and F91L. The two antibodies show large differences in the orientations of their variable and constant domains, reflected by a 32 degrees difference in their elbow angles. The VL and VH domains in the two antibodies differ by a rotation of 8.8 degrees. The hapten binds in similar orientations and locations in 29G11 and 17E8, which appear to have catalytic groups in common, though the changes in the association of the variable domains affect the precise positioning of residues in the hapten-binding pocket.
About this StructureAbout this Structure
1A0Q is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
A comparison of the crystallographic structures of two catalytic antibodies with esterase activity., Buchbinder JL, Stephenson RC, Scanlan TS, Fletterick RJ, J Mol Biol. 1998 Oct 9;282(5):1033-41. PMID:9753552 Page seeded by OCA on Fri May 2 09:38:26 2008