Modeling protein interactions and complexes in CAPRI: Seventh CAPRI evaluation meeting, April 3-5 EMBL-EBI, Hinxton, UK.
Modeling protein interactions and complexes in CAPRI: Seventh CAPRI evaluation meeting, April 3-5 EMBL-EBI, Hinxton, UK.
复制标题
在 CAPRI 中模拟蛋白质相互作用和复合物：第七次 CAPRI 评估会议，4 月 3 日至 5 日 EMBL-EBI，英国欣克斯顿。
作者：
Wodak SJ
The crucial role in all cellular processes played by protein complexes, and more generally by protein interactions with other macromolecules underlie fundamental biological functions, and their deregulation or disruption causes disease. Characterizing protein interactions and understanding their underlying principles, is therefore a major goal of present-day molecular biology and medicine. A substantial part of our knowledge about protein interactions and protein complexes has been derived from data on the threedimensional (3D) structures of these complexes determined by experimental techniques such as X-ray crystallography. So far, however, detailed structural information has been available for only a small fraction of the protein assemblies in the cell that can be detected by proteomics and other methods. On the other hand, structural biology has been very effective in mapping out the structural repertoire of individual proteins, many of which represent building blocks of larger complexes. Computational methods for predicting the structure of protein complexes, which exploit the rapidly increasing body of data on sequences and 3D structures of individual proteins and their complexes stored in public databases, therefore play an increasingly important role in efforts to populate the still uncharted landscape of protein assemblies.The Critical Assessment of Predicted Interactions (CAPRI)(http://www. ebi. ac. uk/msd-srv/capri/; capri-docking. org) has been a major factor fueling progress in this endeavor. CAPRI is a community-wide initiative established in 2001, which offers computational biologists the possibility to test their modeling algorithms in blind prediction Rounds on experimentally-determined structures of protein complexes, the “targets,” provided to CAPRI prior to publication. These prediction Rounds are initiated on a rolling basis, as soon as one or more targets become available, and completed 3 to 6 weeks later. Registered participants are invited to predict the 3D structure of the target protein assembly using as input sequence information alone, or structures of the unbound components when those are available. CAPRI Rounds also include a scoring challenge in which the correct assembly mode (s) must be identified out of an ensemble of decoys (incorrect models). Groups can participate in either or both challenges (as predictors and scorers). Detailed information on how CAPRI Rounds are conducted, how predicted complexes are evaluated against the target structure, and how the performance of participating groups is ranked can be found at www. capri-docking. org and
