UMass Chan Affiliations
Program in Bioinformatics and Integrative BiologyDocument Type
Journal ArticlePublication Date
2020-01-29Keywords
ZRANKcomplex
docking
protein-protein interaction
structure
Amino Acids, Peptides, and Proteins
Biochemistry, Biophysics, and Structural Biology
Bioinformatics
Computational Biology
Metadata
Show full item recordAbstract
We report docking performance on the six targets of Critical Assessment of PRedicted Interactions (CAPRI) rounds 39-45 that involved heteromeric protein-protein interactions and had the solved structures released since the rounds were held. Our general strategy involved protein-protein docking using ZDOCK, reranking using IRAD, and structural refinement using Rosetta. In addition, we made extensive use of experimental data to guide our docking runs. All the experimental information at the amino-acid level proved correct. However, for two targets, we also used protein-complex structures as templates for modeling interfaces. These resulted in incorrect predictions, presumably due to the low sequence identity between the targets and templates. Albeit a small number of targets, the performance described here compared somewhat less favorably with our previous CAPRI reports, which may be due to the CAPRI targets being increasingly challenging.Source
Vreven T, Vangaveti S, Borrman TM, Gaines JC, Weng Z. Performance of ZDOCK and IRAD in CAPRI rounds 39-45. Proteins. 2020 Jan 29. doi: 10.1002/prot.25873. Epub ahead of print. PMID: 31994784. Link to article on publisher's site
DOI
10.1002/prot.25873Permanent Link to this Item
http://hdl.handle.net/20.500.14038/25875PubMed ID
31994784Related Resources
ae974a485f413a2113503eed53cd6c53
10.1002/prot.25873