title: Analysis of the antibody structure based on high-resolution crystallographic studies.
abstract: High-resolution structures of liganded and unliganded antibody molecules were analyzed in terms of the interaction between the antibody with ligand, between the residues in the contact between the variable domains, and between the framework and the complementarity-determining regions of the antibody. The solvent accessibilities of the residues in the variable domains were also analyzed. The structural information is useful in the engineering of antibodies for therapeutic and other purposes.
authors.affiliation: The Marine Science Institute, University of the Philippines Diliman, Quezon City 1101, Philippines.
authors.forename: Jo Erika T
authors.initials: JE
authors.lastname: Narciso
authors.forename: Iris Diana C
authors.initials: ID
authors.lastname: Uy
authors.forename: April B
authors.initials: AB
authors.lastname: Cabang
authors.forename: Jenina Faye C
authors.initials: JF
authors.lastname: Chavez
authors.forename: Juan Lorenzo B
authors.initials: JL
authors.lastname: Pablo
authors.forename: Gisela P
authors.initials: GP
authors.lastname: Padilla-Concepcion
authors.forename: Eduardo A
authors.initials: EA
authors.lastname: Padlan
mesh_terms: D000818:Animals; D000906:Antibodies / Q000737:chemistry* / Q000276:immunology / Q000627:therapeutic use; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D015202:Protein Engineering
chemical_list: D000906:Antibodies