VOLUME 5 NUMBER 1 (January to June 2012)

Phil. Sci. Lett. 2013 5 (1) 063-089
available online: May 29, 2012

*Corresponding author
Email Address: gpconcepcion@gmail.com
Submitted: December 14, 2011
Revised: December 30, 2011
Accepted: December 30, 2011

REVIEW

Anatomy of the antibody molecule: acontinuing analysis based on high-resolutioncrystallographic structures

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.

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