Abstract | ||
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Immunoglobulin molecules specifically recognize particular areas on the surface of proteins. These areas are commonly dubbed B-cell epitopes. The identification of epitopes in proteins is important both for the design of experiments and vaccines. Additionally, the interactions between epitopes and antibodies have often served as a model for protein protein interactions. One of the main obstacles in creating a database of antigen-antibody interactions is the difficulty in distinguishing between antigenic and non-antigenic interactions. Antigenic interactions involve specific recognition sites on the antibody's surface, while non-antigenic interactions are between a protein and any other site on the antibody. To solve this problem, we performed a comparative analysis of all protein-antibody complexes for which structures have been experimentally determined. Additionally, we developed a semi-automated tool that identified the antigenic interactions within the known antigen-antibody complex structures. We compiled those interactions into Epitome, a database of structure-inferred antigenic residues in proteins. Epitome consists of all known antigen/antibody complex structures, a detailed description of the residues that are involved in the interactions, and their sequence/structure environments. Interactions can be visualized using an interface to Jmol. The database is available at http://www.rostlab.org/services/epitome/. |
Year | DOI | Venue |
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2006 | 10.1093/nar/gkj053 | NUCLEIC ACIDS RESEARCH |
Keywords | Field | DocType |
complex structure,immunoglobulin,protein protein interaction,design of experiment | Complementarity determining region,Epitope,Antigen,Biology,Epitome,Molecular biology,Database | Journal |
Volume | Issue | ISSN |
34 | Database issue | 0305-1048 |
Citations | PageRank | References |
11 | 1.94 | 7 |
Authors | ||
4 |
Name | Order | Citations | PageRank |
---|---|---|---|
Avner Schlessinger | 1 | 77 | 6.49 |
Yanay Ofran | 2 | 182 | 14.01 |
Guy Yachdav | 3 | 115 | 10.71 |
Burkhard Rost | 4 | 795 | 88.14 |