VOLUME 5 NUMBER 1 (January to June 2012)

by Jo Erika T. Narciso, Iris Diana C. Uy, April B. Cabang,Jenina Faye C. Chavez, Juan Lorenzo B. Pablo,Gisela P. Padilla-Concepcion*, Eduardo A. Padlan

Currently available high-resolutioncrystallographic studies of liganded andunliganded antibody molecules have provided theopportunity to analyze in more detail the structureof the antibody and its interaction with antigen, aswell as the interactions between the domains of the molecule andbetween the framework and the complementarity-determiningregions of the variable domains. The structural data nowavailable have also allowed a more detailed analysis of thesolvent accessibilities of the residues in the various domains ofthe molecule. The information resulting from this analysis isuseful in the engineering of antibodies for therapeutic and otherpurposes.