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- W2978249885 endingPage "e1007193" @default.
- W2978249885 startingPage "e1007193" @default.
- W2978249885 abstract "Guanylate binding proteins (GBPs) belong to the dynamin-related superfamily and exhibit various functions in the fight against infections. The functions of the human guanylate binding protein 1 (hGBP1) are tightly coupled to GTP hydrolysis and dimerization. Despite known crystal structures of the hGBP1 monomer and GTPase domain dimer, little is known about the dynamics of hGBP1. To gain a mechanistic understanding of hGBP1, we performed sub-millisecond multi-resolution molecular dynamics simulations of both the hGBP1 monomer and dimer. We found that hGBP1 is a highly flexible protein that undergoes a hinge motion similar to the movements observed for other dynamin-like proteins. Another large-scale motion was observed for the C-terminal helix α13, providing a molecular view for the α13-α13 distances previously reported for the hGBP1 dimer. Most of the loops of the GTPase domain were found to be flexible, revealing why GTP binding is needed for hGBP1 dimerization to occur." @default.
- W2978249885 created "2019-10-10" @default.
- W2978249885 creator A5011523143 @default.
- W2978249885 creator A5036143399 @default.
- W2978249885 creator A5054994539 @default.
- W2978249885 date "2019-10-07" @default.
- W2978249885 modified "2023-10-15" @default.
- W2978249885 title "Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations" @default.
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- W2978249885 doi "https://doi.org/10.1371/journal.pcbi.1007193" @default.
- W2978249885 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6797221" @default.
- W2978249885 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31589600" @default.
- W2978249885 hasPublicationYear "2019" @default.
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