RING box protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<StructureSection load='4f52' size='340' side='right' caption='Human RING finger protein 1 (green and yellow) complex with cullin-1 (grey and pink), glomulin (magenta and cyan) and Zn+2 ions (grey) (PDB code [[4f52]])' scene=''>
+
<StructureSection load='4f52' size='340' side='right' caption='Human RING finger protein 1 (green) complex with cullin-1 (grey), glomulin (magenta) and Zn+2 ions (grey) (PDB code [[4f52]])' scene=''>
'''RING box protein''' (RBX) makes a heterodimer with cullin. The heterodimer is essential for the protein ubiquitination process. RBX1 is a component of the SCF (Skp1-cullin-F box protein) E3 ubiquitin ligase complex. RBX contains a RING-type zinc finger domain. The RING domain is 40 to 60 residues long and binds two Zn atoms. It is involved in protein-protein interaction.
'''RING box protein''' (RBX) makes a heterodimer with cullin. The heterodimer is essential for the protein ubiquitination process. RBX1 is a component of the SCF (Skp1-cullin-F box protein) E3 ubiquitin ligase complex. RBX contains a RING-type zinc finger domain. The RING domain is 40 to 60 residues long and binds two Zn atoms. It is involved in protein-protein interaction.

Revision as of 09:10, 17 August 2016

Human RING finger protein 1 (green) complex with cullin-1 (grey), glomulin (magenta) and Zn+2 ions (grey) (PDB code 4f52)

Drag the structure with the mouse to rotate

3D Structures of RING box protein

Updated on 17-August-2016

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

Personal tools