Philippine Science Letters
vol. 5 | no. 1 | 2012
published online May 29, 2012


REVIEW


Anatomy of the antibody molecule: a continuing analysis based on high-resolution crystallographic 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



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Currently available high-resolution crystallographic studies of liganded and unliganded antibody molecules have provided the opportunity to analyze in more detail the structure of the antibody and its interaction with antigen, as well as the interactions between the domains of the molecule and between the framework and the complementarity-determining regions of the variable domains. The structural data now available have also allowed a more detailed analysis of the solvent accessibilities of the residues in the various domains of the molecule. The information resulting from this analysis is useful in the engineering of antibodies for therapeutic and other purposes.