1mie: Difference between revisions

Revision as of 00:02, 3 July 2008

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File:1mie.png

Template:STRUCTURE 1mie

Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393

Template:ABSTRACT PUBMED 12948492

About this StructureAbout this Structure

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

Page seeded by OCA on Thu Jul 3 00:02:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393'''
+===Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12948492}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12948492 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12948492}}
 ==About this Structure==
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 [[Category: Fab]]
 [[Category: Immunoglobulin]]
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