EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.7.4.8 | more |
As is evident from the structure, GK has a clamp-like cavity, where the two lobes of the protein close through an ca. 1-nm conformational change upon binding the substrates, most of the conformational motion is induced by GMP binding. The substrates GMP and ATP drive this conformational change through several direct and indirect (via water molecules) interactions that bring the LID and nucleotide-monophosphate-binding domain (herein referred to as NMP-BD) nearer and jointly toward the CORE region, the structure closing in a vise-like motion. In this configuration, the CORE is catalytically active toward phosphoryl transfer, which relies on a residue sequence (the P-loop) that is conserved in kinases. |
672643 |
| 2.7.4.8 | phosphoprotein |
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation through Ser/Thr protein kinases and also Tyr-dependent kinases, overview |
700475 |
| 2.7.4.8 | phosphoprotein |
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation, through Ser/Thr protein kinases and also Tyr-dependent kinases, overview |
700475 |
