Polyubiquitin b: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
Ubiquitin has lots of lysine residues throughout the protein. The lysine residues play a large part in the binding ability of the protein due to its basic properties. It is made up of three domains with a total of 229 residues. The TRAF6 RING dimer forms a catalytic complex with RING interacting with the Ubiquitin conjugate and a zinc finger domain that opposes it in the Ubiquitin contact. The TRAF5 enables Ubiquitin to transfer from a TRAF6 bound conjugate. The TRAF RING domains can synthesize Ubiquitin chains for tagging the cellular proteins for degradation. <ref> PMID: 19489726</ref> | Ubiquitin has lots of lysine residues throughout the protein. The lysine residues play a large part in the binding ability of the protein due to its basic properties. It is made up of three domains with a total of 229 residues. The TRAF6 RING dimer forms a catalytic complex with RING interacting with the Ubiquitin conjugate and a zinc finger domain that opposes it in the Ubiquitin contact. The TRAF5 enables Ubiquitin to transfer from a TRAF6 bound conjugate. The TRAF RING domains can synthesize Ubiquitin chains for tagging the cellular proteins for degradation. <ref> PMID: 19489726</ref> | ||
<scene name='77/778330/Poly/1'>Ubiquitin</scene> | |||
Clicking on the <scene name='77/778330/Lysine_ubiquitin/1'>Show lysines</scene> link will show the active site lysines in space fill (CPK color) | Clicking on the <scene name='77/778330/Lysine_ubiquitin/1'>Show lysines</scene> link will show the active site lysines in space fill (CPK color) | ||
