Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode
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Publisher
New York: Nature Publishing Group US
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Language
English
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New York: Nature Publishing Group US
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Contents
Human OGA forms an unusual arm-in-arm homodimer with a substrate-binding cleft that affords extensive interactions with the peptide substrate in a recognition mode distinct from that of its bacterial homologs.
Human O-GlcNAcase (hOGA) is the unique enzyme responsible for the hydrolysis of the O-linked β-
N
-acetyl glucosamine (O-GlcNAc) mo...
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Full title
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8171356
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8171356
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/nsmb.3390
