Journal
NUCLEIC ACIDS RESEARCH
Volume 43, Issue D1, Pages D283-D289Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku1119
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Funding
- Hungarian Scientific Research Fund [K104586]
- Hungarian Academy of Sciences [LP2012-35]
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The Topology Data Bank of Transmembrane Proteins (http://topdb.enzim.ttk.mta.hu) contains experimentally determined topology data of transmembrane proteins. Recently, we have updated TOPDB from several sources and utilized a newly developed topology prediction algorithm to determine the most reliable topology using the results of experiments as constraints. In addition to collecting the experimentally determined topology data published in the last couple of years, we gathered topographies defined by the TMDET algorithm using 3D structures from the PDBTM. Results of global topology analysis of various organisms as well as topology data generated by high throughput techniques, like the sequential positions of N- or O-glycosylations were incorporated into the TOPDB database. Moreover, a new algorithm was developed to integrate scattered topology data from various publicly available databases and a new method was introduced to measure the reliability of predicted topologies. We show that reliability values highly correlate with the per protein topology accuracy of the utilized prediction method. Altogether, more than 52 000 new topology data and more than 2600 new transmembrane proteins have been collected since the last public release of the TOPDB database.
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