User:Alan Moreira Henrique/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 20: Line 20:
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
-
Parkin is a monomeric 465-residues long protein containing an <scene name='81/817545/Ubl_domain/1'>Ubiquitin-like (Ubl) Domain</scene>, a RING0 domain, a RING1 domain, an In Between Rings (IBR) domain, a repressor (REP) element and a RING2 domain. Parkin is produced by the cell in an autoinhibited state. The Ubl domain maintains a compact RING0-RING1 interface. Phosphorylation of the Ser65 residue in the Ubl domain leads to a change in conformation in the tertiary structure of the protein in the RING0-RING1 interface, which is optimized for pUb binding. However, both pUb and pUbl cannot be bound to parkin at the same time, which is consistent with the proposed allosteric loss of structure to the C-terminus of Helix H3 and IBR domain that would interfere with the Ubl-binding site.
+
Parkin is a monomeric 465-residues long protein containing an Ubiquitin-like (Ubl) Domain, a RING0 domain, a RING1 domain, an In Between Rings (IBR) domain, a <scene name='81/817543/Rep/1'>repressor (REP) element</scene> and a RING2 domain. Parkin is produced by the cell in an autoinhibited state. The <scene name='81/818543/Ubl/1'>Ubl domain</scene> maintains a compact RING0-RING1 interface. Phosphorylation of the Ser65 residue in the Ubl domain leads to a change in conformation in the tertiary structure of the protein in the RING0-RING1 interface, which is optimized for pUb binding. However, both pUb and pUbl cannot be bound to parkin at the same time, which is consistent with the proposed allosteric loss of structure to the C-terminus of Helix H3 and IBR domain that would interfere with the Ubl-binding site.
</StructureSection>
</StructureSection>

Revision as of 22:09, 16 June 2019

Parkin

Parkin (PDB code: 5c1z)

Drag the structure with the mouse to rotate

References

Kumar, A., Aguirre, J.D., Condos, T.E., Martinez-Torres, R.J., Chaugule, V.K., Toth, R., Sundaramoorthy, R., Mercier, P., Knebel, A., Spratt, D.E., Barber, K.R., Shaw, G.S., Walden, H. Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis. (2015) Embo J. 34: 2506-2521

Proteopedia Page Contributors and Editors (what is this?)

Alan Moreira Henrique

Personal tools