Sandbox Reserved 1656: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 18: | Line 18: | ||
==== Localization ==== | ==== Localization ==== | ||
The localization depends on the DUB we consider. | The localization depends on the DUB we consider. Nevertheless, the majority of DUBs are found in the nucleus, plasma membrane and/or in secretory and endocytic pathways. For example, in the ubiquitin-specific proteases family (UPSs), USP21 is mostly associated with microtubules and the [https://en.wikipedia.org/wiki/Centrosome centrosome]. Thus this deubiquitinase is highly dependent on all the physiological mechanisms involving the [https://en.wikipedia.org/wiki/Microtubule microtubules]. <ref>PMID:22298430</ref> | ||
== Structure == | == Structure == | ||
| Line 24: | Line 24: | ||
==== The overall structure ==== | ==== The overall structure ==== | ||
3TMP is the catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde. It is a 8 chain structure with | 3TMP is the catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde. It is a 8-chain-structure with sequences from Human. Indeed, 3TMP is made of two macromolecules : OTU domain-containing protein 5 (also named DUBA or OTUD5) and Polyubiquitin-C, which is the ubiquitin aldehyde. The catalytic domain is also composed of two small molecules the phosphoserine (SEP) and the amino-acetaldehyde (GLZ),which they are L-peptide links. <ref>PMID:22245969</ref> | ||
=== Impact of phosphorylation on DUB activity === | === Impact of phosphorylation on DUB activity === | ||
Evidence shows that phosphorylation influences activity | Evidence shows that phosphorylation influences enzyme activity. Phosphorylated serine seems to have the most influence on the enzyme activity <scene name='86/868189/Ser177/1'>especially on Ser177</scene>. The phosphorylation of this nucleotide is crucial to the protein to work. | ||
In fact, this part bends to welcome the protein to be | In fact, this part bends to welcome the protein to be deubiquitinated. <ref>PMID:22245969</ref> | ||
==== Catalytic domain ==== | ==== Catalytic domain ==== | ||