PMID: 9530559Apr 8, 1998Paper

Three-dimensional structure of a human Fab with high affinity for tetanus toxoid

Immunotechnology : an International Journal of Immunological Engineering
C FaberA B Edmundson

Abstract

The wide range of antibody specificity and affinity results from the differing shapes and chemical compositions of their binding sites. These shapes range from discrete grooves in antibodies elicited by linear oligomers of nucleotides and carbohydrates to shallow depressions or flat surfaces for accommodation of proteins, peptides and large organic compounds. To determine the Fab structure of a high-affinity human antitoxin antibody. To explore structural features which enable the antibody to bind to intact tetanus toxoid, peptides derived from the sequence of the natural immunogen and antigenic mimics identified by combinatorial chemistry. To explain why this Fab shows a remarkable tendency to produce crystals consistently diffracting to d spacings of 1.7-1.8 A. To use this information to engineer a strong tendency to crystallize into the design of other Fabs. The protein was crystallized in hanging or sitting drops by a microseeding technique in polyethylene glycol (PEG) 8000. Crystals were subjected to X-ray analysis and the three-dimensional structure of the Fab was determined by the molecular replacement method. Interactive computer graphics were employed to fit models to electron density maps, survey the structure in mult...Continue Reading

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Citations

Aug 14, 2001·Journal of Molecular Recognition : JMR·A B EdmundsonP A Ramsland
Nov 26, 2002·Journal of Molecular Recognition : JMR·Allen B Edmundson
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Sep 20, 2019·Protein Engineering, Design & Selection : PEDS·Rob van der KantJoost Schymkowitz

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