Sandbox Reserved 381: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
Line 24: Line 24:


== OGT Structure ==
== OGT Structure ==
OGT is comprised of two distinct regions: a multidomain catalytic region, which has no available structure and an N-terminal region consisting of a seris of tetratricopeptide repeat(TPR)units.<ref>PMID:9083067</ref>  The N terminus of OGT is unusual, consisting of 2.5-13.5 tetratricopeptide repeats (TPRs) depending on alternative splicing.<ref>Kreppel L, Hart G. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem. 1999;274:32015-32022</ref> The N-terminal domain of tetratricopeptide (TPR)  mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope.   
OGT is comprised of two distinct regions: a multidomain catalytic region, which has no available structure and an N-terminal region consisting of a seris of tetratricopeptide repeat(TPR) units.<ref>PMID:9083067</ref>  The N terminus of OGT is unusual, consisting of 2.5-13.5 tetratricopeptide repeats (TPRs) depending on alternative splicing.<ref>Kreppel L, Hart G. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem. 1999;274:32015-32022</ref> The N-terminal domain of tetratricopeptide (TPR)  mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope.