Ku protein: Difference between revisions
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=== α/β-Domain === | === α/β-Domain === | ||
Contained inside the <scene name='56/567269/Ku70_dimer/2'>α/β-Domain</scene> is a [[Rossman fold]] at the N terminus that is used to bind nucleotides in | Contained inside the <scene name='56/567269/Ku70_dimer/2'>α/β-Domain</scene> is a [[Rossman fold]] at the N terminus that is used to bind nucleotides in DNA.<ref name="Walker"/> | ||
In terms of protein structure, the | In terms of protein structure, the α/β-Domain contributes little to the dimer interface between the subunits. | ||
The C terminus of the domain can be bound to other repair molecules, using | The C terminus of the domain can be bound to other repair molecules, using the α/β-Domain as a scaffold.<ref name="Walker"/> | ||
=== β-barrel === | === β-barrel === | ||
The <scene name='56/567269/Ku70_dimer/4'>β-barrel</scene> is the main source of interactions of the | The <scene name='56/567269/Ku70_dimer/4'>β-barrel</scene> is the main source of interactions of the Ku heterodimer itself and DNA helix, with each β-barrel being composed of seven β strands with the majority in antiparallel arrangement.<ref name="Walker"/> | ||
The quantity of the strands lends the structures to be symmetrical. Both | The quantity of the strands lends the structures to be symmetrical. Both β-barrel in the dimer form the base of the cradle by fitting in the grooves of DNA. | ||
=== C-terminal arm === | === C-terminal arm === | ||
The <scene name='56/567269/Ku70_dimer/7'>C-terminal arm</scene> is an α-helical domain that associates with the β-barrel of the opposite subunit, with the arm stretching across the | The <scene name='56/567269/Ku70_dimer/7'>C-terminal arm</scene> is an α-helical domain that associates with the β-barrel of the opposite subunit, with the arm stretching across the DNA helix.<ref name="Walker"/> | ||
As a result, the | As a result, the C-terminal arm strengthens the cradle composed of the two β-barrels. | ||
