Analysis of the antibody structure based on high-resolution crystallographic studies

被引：34

作者：

Narciso, Jo Erika T. ^{[1
]}

Uy, Iris Diana C. ^{[1
]}

Cabang, April B. ^{[1
]}

Chavez, Jenina Faye C. ^{[1
]}

Pablo, Juan Lorenzo B. ^{[1
]}

Padilla-Concepcion, Gisela P. ^{[1
]}

Padlan, Eduardo A. ^{[1
]}

机构：

[1] Univ Philippines Diliman, Inst Marine Sci, Quezon City 1101, Philippines

来源：

NEW BIOTECHNOLOGY | 2011年 / 28卷 / 05期

关键词：

SINGLE-DOMAIN ANTIBODY; ANGSTROM RESOLUTION; HUMAN-IMMUNOGLOBULIN; AFFINITY MATURATION; CRYSTAL-STRUCTURES; FAB FRAGMENT; HIV-1; GP120; BINDING; COMPLEX; ANTIGEN;

D O I：

10.1016/j.nbt.2011.03.012

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：435 / 447

页数：13

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