![]() ![]() ![]() To address this problem, we have developed a Structural Antibody Database (SAbDab), a database devoted to automatically collecting, curating and presenting antibody structural data in a consistent manner for both bulk analysis and individual inspection. Neither allow for the generation of bespoke datasets nor for the download of an ensemble of curated structural data. In comparison, both IMGT ( 9) and the Abysis portal ( 10) provide the ability to inspect and download individual bound and unbound antibody structures. However, both focus on collecting epitope data and do not include unbound antibody structures. AntigenDB ( 11) and IEDB-3D ( 12) do include structural data. However, it does not incorporate structural data. The most recent, DIGIT ( 13), provides sequence information for immunoglobulins and has the advantage over earlier sequence databases of providing heavy and light chain sequence pairings. Of these, most are sequence-based or are antibody discovery tools. Several databases that handle antibody data currently exist ( 7–13). However, since the first antibody structure was deposited in 1976 ( 5), the number of antibody structures in the protein data bank (PDB) ( 6) has grown, and it now represents approximately 1.75% of the total 91939 entries (July 2013). The publicly available structural data for most types of proteins are too sparse to merit protein-specific prediction methods. Many of these tools now use only the antibody data, as opposed to general protein data, because this has been shown to increase performance ( 3, 4). This biopharmaceutical application has motivated the desire to understand how binding, stability and immunogenic properties of the antibody are determined and how they can be modified.Ĭomputational analyses and tools are increasingly being employed to aid the antibody engineering process ( 2). ![]() In addition to the biological importance of antibodies, their ability to be raised against an almost limitless number of molecules has made them useful laboratory tools and increasingly useful as therapeutic agents in humans ( 1). These proteins form complexes with potentially pathogenic molecules called antigens and inhibit their function or recruit other components of the immunological machinery to destroy them. Antibodies form the foundations of the vertebrate immune response. ![]()
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