Sandbox Reserved 381: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
Line 19: Line 19:
== OGT Features of Interest ==
== OGT Features of Interest ==


OGT is the only known member to glycosylate polypeptides and it contains a long uncharacterized intervening sequence (~120 amino acids) in the middle of the catalytic region.  Studies suggest that OGT contains a phosphatidylinositol (3,4,5)-trisphosphate (PIP3)binding domain.  The most unusual feature of OGT is the intervening domain between the catalytic lobes, which is only found in metazoans.  This polypeptide adopts a topologically novel fold with a seven-stranded <scene name='Sandbox_Reserved_381/Ogt_structure/1'>beta</scene> sheet core stabilized by flanking alpha helices.  There are two long unstructured loops for which electron density is missing.<ref> PMID:18288188</ref>
OGT is the only known member to glycosylate polypeptides and it contains a long uncharacterized intervening sequence (~120 amino acids) in the middle of the catalytic region.  Studies suggest that OGT contains a phosphatidylinositol (3,4,5)-trisphosphate (PIP3)binding domain.  The most unusual feature of OGT is the intervening domain between the catalytic lobes, which is only found in metazoans.  This polypeptide adopts a topologically novel fold with a seven-stranded <scene name='Sandbox_Reserved_381/Ogt_structure/1'>beta</scene> sheet core stabilized by flanking alpha helices.  There are two long <scene name='Sandbox_Reserved_381/Unstructured_loops/1'>unstructured loops</scene> for which electron density is missing.<ref> PMID:18288188</ref>