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Literature summary for 2.4.1.255 extracted from

  • Pathak, S.; Alonso, J.; Schimpl, M.; Rafie, K.; Blair, D.; Borodkin, V.; Schttelkopf, A.; Albarbarawi, O.; Van Aalten, D.
    The active site of O-GlcNAc transferase imposes constraints on substrate sequence (2015), Nat. Struct. Mol. Biol., 22, 744-749.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
analysis application of a high-throughput OGT assay to a library of peptides Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
cocrystallization of identified substrate peptides with OGT, derived from retinoblastoma-like protein 2 (RBL2411-422, KENPAVTPVSTA), proto-oncogene tyrosine protein kinase receptor Ret (Ret660-672, AQAFPVSYSSSGA), keratin-7 (KER77-19, SPVFTSRSAAFSC) and lamin B1 (LAMIN179-191, KLSPSPSSRVTVS). The peptide is teth­ered into a common binding mode by a combination of van der Waals interactions and hydrogen bonds that restrict torsional freedom in the -3 to +2 subsites only Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15294
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a combination of size and conformational restriction defines sequence specificity in the -3 to +2 subsites of O-GlcNAc modification. Although the N-terminal tetratricopeptide repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity Homo sapiens ?
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