期刊
NUCLEIC ACIDS RESEARCH
卷 34, 期 -, 页码 D777-D780出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkj053
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资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM064633] Funding Source: NIH RePORTER
- NATIONAL LIBRARY OF MEDICINE [R01LM007329] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM064633, R01-GM64633-01] Funding Source: Medline
- NLM NIH HHS [R01 LM007329, R01-LM07329-01] Funding Source: Medline
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/.
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