Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 87, Issue 12, Pages 1190-1199Publisher
WILEY
DOI: 10.1002/prot.25795
Keywords
CASP; protein assembly; protein interfaces; structure prediction
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Funding
- Division of Biological Infrastructure [1832184]
- National Institute of General Medical Sciences [GM100482]
- Div Of Biological Infrastructure
- Direct For Biological Sciences [1832184] Funding Source: National Science Foundation
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We present the assembly category assessment in the 13th edition of the CASP community-wide experiment. For the second time, protein assemblies constitute an independent assessment category. Compared to the last edition we see a clear uptake in participation, more oligomeric targets released, and consistent, albeit modest, improvement of the predictions quality. Looking at the tertiary structure predictions, we observe that ignoring the oligomeric state of the targets hinders modeling success. We also note that some contact prediction groups successfully predicted homomeric interfacial contacts, though it appears that these predictions were not used for assembly modeling. Homology modeling with sizeable human intervention appears to form the basis of the assembly prediction techniques in this round of CASP. Future developments should see more integrated approaches where subunits are modeled in the context of the assemblies they form.
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