Sandbox Reserved 827: Difference between revisions
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=Overall structure= | =Overall structure= | ||
< | <Structure load='4IW0' size='430' frame='true' align='right' caption='TBK1 monomer (PDB entry 4IW0)' scene='56/568025/Vide/1' /> | ||
==Protomer== | ==Protomer== | ||
'''Kinase domain :''' ( <scene name='56/568025/Kd/1'>KD</scene> ) from amino acid 9 to amino acid 310: the active site is at the interface of the N- and C-terminal lobes. | '''Kinase domain :''' (<scene name='56/568025/Kd/1'>KD</scene>) from amino acid 9 to amino acid 310: the active site is at the interface of the N- and C-terminal lobes. | ||
Inactive conformation: the C-helix and key residue Glu55 displaced from the active site. | Inactive conformation: the C-helix and key residue Glu55 displaced from the active site. | ||
Active conformation: a rotation of the C-helix allows a key salt-bridge interaction between conserved glutamic acid in the C-helix and an active-site lysine residue. | Active conformation: a rotation of the C-helix allows a key salt-bridge interaction between conserved glutamic acid in the C-helix and an active-site lysine residue. | ||
The DFG (Asp-Phe-Gly) motif and Ser172 are involved in the regulation of the kinase activity. | The DFG (Asp-Phe-Gly) motif and Ser172 are involved in the regulation of the kinase activity. | ||
'''Ubiquitin-like domain :''' ( <scene name='56/568025/Uld/1'>UBL</scene> ) from amino acid 309 to amino acid 385: it contains five β strands which form a hydrophobic interface, giving the protein a high structural homology with ubiquitin. | '''Ubiquitin-like domain :''' (<scene name='56/568025/Uld/1'>UBL</scene>) from amino acid 309 to amino acid 385: it contains five β strands which form a hydrophobic interface, giving the protein a high structural homology with ubiquitin. | ||
The '''<scene name='56/568025/Lz/1'>leucine zipper</scene> ''' (between amino acid 408 and amino acid 651) and the '''coiled coil domain ''' (between amino acid 408 and amino acid 651) are responsible for the dimerization of the protomer. Together they form the '''scaffolding dimerization domain''' (SDD). This domain presents many alpha-helix. | The '''<scene name='56/568025/Lz/1'>leucine zipper</scene> ''' (between amino acid 408 and amino acid 651) and the '''coiled coil domain ''' (between amino acid 408 and amino acid 651) are responsible for the dimerization of the protomer. Together they form the '''scaffolding dimerization domain''' (SDD). This domain presents many alpha-helix. | ||
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UBL and KD also contribute to dimerization thanks to several interactions with the SDD of the opposite subunit in the homodimer. | UBL and KD also contribute to dimerization thanks to several interactions with the SDD of the opposite subunit in the homodimer. | ||
There are several hydrogen bonds between the KD (N- and C-lobes) and the SDD of the opposite subunit: a salt bridge is formed between Asp33 in the N-lobe and Lys589 in the SDD and the strands the β7-β8 in the C-love interact with the SDD. A “EGR” sequence (residues 355–357) in the UBL interacts with the SDD: Glu355-UBL interacts with Arg444-SDD (salt bridge) and Trp445-SDD (hydrogen bonds). | There are several hydrogen bonds between the KD (N- and C-lobes) and the SDD of the opposite subunit: a salt bridge is formed between Asp33 in the N-lobe and Lys589 in the SDD and the strands the β7-β8 in the C-love interact with the SDD. A “EGR” sequence (residues 355–357) in the UBL interacts with the SDD: Glu355-UBL interacts with Arg444-SDD (salt bridge) and Trp445-SDD (hydrogen bonds). | ||
=Possible residue modifications= | =Possible residue modifications= | ||
<Structure load='4IW0' size=' | <Structure load='4IW0' size='430' frame='true' align='right' caption='TBK1 monomer (PDB entry 4IW0)' scene='56/568025/Vide/1' /> | ||
Several residues of TBK1 can be modified, by phosphorylation or polyubiquitination. | Several residues of TBK1 can be modified, by phosphorylation or polyubiquitination. | ||
