TY  - JOUR
AU  - Soh, Timothy K.
AU  - Ognibene, Sofia
AU  - Sanders, Saskia
AU  - Schäper, Robin
AU  - Kaufer, Benedikt B.
AU  - Bosse, Jens Bernhard
TI  - A proteome-wide structural systems approach reveals insights into protein families of all human herpesviruses
JO  - Nature Communications
VL  - 15
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - PUBDB-2024-08047
SP  - 10230
PY  - 2024
AB  - Structure predictions have become invaluable tools, but viral proteins are absent from the EMBL/DeepMind AlphaFold database. Here, we provide proteome-wide structure predictions for all nine human herpesviruses and analyze them in depth with explicit scoring thresholds. By clustering these predictions into structural similarity groups, we identified new families, such as the HCMV UL112-113 cluster, which is conserved in alpha- and betaherpesviruses. A domain-level search found protein families consisting of subgroups with varying numbers of duplicated folds. Using large-scale structural similarity searches, we identified viral proteins with cellular folds, such as the HSV-1 US2 cluster possessing dihydrofolate reductase folds and the EBV BMRF2 cluster that might have emerged from cellular equilibrative nucleoside transporters. Our HerpesFolds database is available at https://www.herpesfolds.org/herpesfolds and displays all models and clusters through an interactive web interface. Here, we show that system-wide structure predictions can reveal homology between viral species and identify potential protein functions. 
LB  - PUB:(DE-HGF)16
C6  - pmid:39592652
UR  - <Go to ISI:>//WOS:001364813000027
DO  - DOI:10.1038/s41467-024-54668-2
UR  - https://bib-pubdb1.desy.de/record/619956
ER  -