標題: ATRIPPI: An atom-residue preference scoring function for protein-protein interactions
作者: Liu, Kang-Ping
Chang, Lu-Shian
Yang, Jinn-Moon
生物科技學系
Department of Biological Science and Technology
關鍵字: protein-protein interaction;atom-atom interacting preference;knowledge-based scoring matrix;residue-residue interaction preference
公開日期: 2009
摘要: We present an ATRIPPI model for analyzing protein-protein interactions. This model is a 167-atom-type and residue-specific interaction preferences with distance bins derived from 641 co-crystallized protein-protein interfaces. The ATRIPPI model is able to yield physical meanings of hydrogen bonding, disulfide bonding, electrostatic interactions, van der Wools and aromatic-aromatic interactions. We applied this model to identify the native states and near-native complex structures on 17 bound and 17 unbound complexes from thousands of decoy structures. On average, 77.5% structures (155 structures) of top rank 200 structures are closed to the native structure. These results suggest that the ATRIPPI model is able to keep the advantages of both atom-atom and residue-residue interactions and is a potential knowledge-based scoring function for protein-protein docking methods. We believe that our model is robust and provides biological meanings to support protein-protein interactions.
URI: http://hdl.handle.net/11536/14677
http://dx.doi.org/10.1109/BIBE.2009.45
ISBN: 978-1-4244-4294-2
DOI: 10.1109/BIBE.2009.45
期刊: 2009 9TH IEEE INTERNATIONAL CONFERENCE ON BIOINFORMATICS AND BIOENGINEERING
起始頁: 392
結束頁: 399
顯示於類別:會議論文


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  1. 000277202300064.pdf