Sandbox Reserved 827: Difference between revisions
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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'> | '''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. | ||
'''<scene name='56/568025/Lz/1'> | 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. | ||
''' | '''ATP binding domain :''' from amino acid 15 to amino acid 23. This is where is bound the ATP needed for the reaction catalyzed by TBK1. This domain is really close to the catalytic residue in the 3D shape of the enzyme. | ||
The KD and the UBL interact with each other: the UBL with the C-lobe of the KD. There is a hydrogen bond between Tyr325 in the ULD and Glu109 in the KD. Moreover Lys323 in the UBL makes favourable electrostatic interactions with Glu109-KD. | |||
The KD and the | |||
==Dimer== | ==Dimer== | ||
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 | 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).</StructureSection> | ||
=Possible residue modifications= | =Possible residue modifications= | ||
