Sandbox Reserved 827: Difference between revisions
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Léa Faivre (talk | contribs) No edit summary |
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=Overall structure= | |||
<StructureSection load='4IW0' size='500' side='right' caption='Structure of TBK1 (PDB entry [[4IW0]])' scene='56/568025/Vide/1'> | |||
==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. | ||
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ULD and KD also contribute to dimerization thanks to several interactions with the SDD of the opposite subunit in the homodimer. | ULD 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 ULD interacts with the SDD: Glu355-ULD 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 ULD interacts with the SDD: Glu355-ULD interacts with Arg444-SDD (salt bridge) and Trp445-SDD (hydrogen bonds).</StructureSection> | ||
= Possible residue modifications = | |||
=Possible residue modifications= | |||
<Structure load='4IW0' size='350' 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. | ||
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'''Polyubiquitination :''' Polyubiquitination in a Lys63 manner on | '''Polyubiquitination :''' Polyubiquitination in a Lys63 manner on | ||
<scene name='56/568025/K30/1'>Lys30</scene> helps the activation of the kinase. The same type of modification on <scene name='56/568025/K401/1'>Lys401</scene> is responsible for dimerization. Type Lys48 polyubiquitination on Lys670 is done by DTX4 and is responsible for the degradation of the protein. | <scene name='56/568025/K30/1'>Lys30</scene> helps the activation of the kinase. The same type of modification on <scene name='56/568025/K401/1'>Lys401</scene> is responsible for dimerization. Type Lys48 polyubiquitination on Lys670 is done by DTX4 and is responsible for the degradation of the protein. | ||
= Signalling pathways = | = Signalling pathways = | ||
