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- W2082836005 abstract "On the loose: We report an STD NMR spectroscopic study of the polysialyltransferase from Neisseria meningitidis serogroup B (NmB-polyST). The spectra reveal that the cytosine and ribose moiety receive more saturation than the sialic acid residue of CMP-Neu5Ac. This loose binding enables a fast and efficient sialyl transfer to the acceptor substrate. Our analysis offers a view of the structural determinants necessary for binding to NmB-polyST that provide the basis for the development of novel NmB-polyST inhibitors." @default.
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- W2082836005 date "2010-01-25" @default.
- W2082836005 modified "2023-09-23" @default.
- W2082836005 title "Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding" @default.
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- W2082836005 doi "https://doi.org/10.1002/cbic.200900659" @default.
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