RING box protein: Difference between revisions

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Revision as of 11:23, 9 July 2015 view source Michal Harel (talk \| contribs) 31,761 edits No edit summary ← Older edit		Revision as of 12:10, 17 August 2016 view source Michal Harel (talk \| contribs) 31,761 edits No edit summary Newer edit →
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	<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.