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The structural diversity and the biological meaning of antibody
Author(s) -
HIFUMI EMI,
AKIYOSHI YUKO,
UDA TAIZO
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb80
Subject(s) - immunoglobulin light chain , antibody , chemistry , domain (mathematical analysis) , function (biology) , dimer , computational biology , biophysics , stereochemistry , evolutionary biology , biology , genetics , mathematics , mathematical analysis , organic chemistry
Along with the development of antibody drugs and catalytic antibodies, the structural diversity issue has attracted much attention. Structural diversity(or structural heterogeneity) is generated caused by the modification of different charges, different molecular sizes, and/or modified amino acid residues. Namely, an antibody takes multi‐molecular forms in the solution. It is desirable that the antibody and/or the subunits must have a defined structure for practical use. Regarding with the difficult issue on the structural diversity of antibody, we found the interesting phenomena in which copper ion can convert the multi‐molecular forms of antibodies to mono‐molecular form (1). The ion hugely contributed to the enrichment of the dimer‐form and the homogenation of the differently charged full‐length of the light chain. The role of copper ion must be significant for preparing a single, defined, not multiple, isoform structure. In addition, we found that the constant region domain (CL) of the antibody light chain also plays an important role in the structural heterogeneity of the light chain (2), which was clarified by expressing the constant domain. Considering the chemical features of the full length light chain (VL+CL) and CL, note that the CL domain can influence to generation of the structural diversity of the VL domain. This finding is important, because, even at the present, the function of CL is still unknown. It is considered that the generation of the structural diversity of a protein may influence on the binding ability as well as the specificity. In the presentation, the authors will discuss not only the reason why antibodies take such structural diversity but also their biological meanings. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .