1mj7
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Crystal Structure Of The Complex Of The Fab fragment of Esterolytic Antibody MS5-393 and A Transition-State Analog
OverviewOverview
The crystal structures of four related Fab fragments of a family of, catalytic antibodies displaying differential levels of esterase activity, have been solved in the presence and in the absence of the, transition-state analogue (TSA) that was used to elicit the immune, response. The electron density maps show that the TSA conformation is, essentially identical, with limited changes on hapten binding., Interactions with the TSA explain the specificity for the D rather than, the L-isomer of the substrate. Differences in the residues in the, hapten-binding pocket, which increase hydrophobicity, appear to correlate, with an increase in the affinity of the antibodies for their substrate., Analysis of the structures at the active site reveals a network of, conserved hydrogen bond contacts between the TSA and the antibodies, and, points to a critical role of two conserved residues, HisL91 and LysH95, in, catalysis. However, these two key residues are set into very different, contexts in their respective structures, with an apparent direct, correlation between the catalytic power of the antibodies and the, complexity of their interactions with the rest of the protein. This, suggests that the catalytic efficiency may be controlled by contacts, arising from a second sphere of residues at the periphery of the active, site.
About this StructureAbout this Structure
1MJ7 is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution crystal structure of the Fab-fragments of a family of mouse catalytic antibodies with esterase activity., Ruzheinikov SN, Muranova TA, Sedelnikova SE, Partridge LJ, Blackburn GM, Murray IA, Kakinuma H, Takahashi-Ando N, Shimazaki K, Sun J, Nishi Y, Rice DW, J Mol Biol. 2003 Sep 12;332(2):423-35. PMID:12948492
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