P53-DNA Recognition: Difference between revisions
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The p53 protein consists of the N-terminal transactivation, the DNA binding or core, the tetramerization, and the C-terminal regulatory domain (Figure 3). This Proteopedia page discusses protein-DNA recognition by p53, thus focuses on the DBD of p53. The only other domain for which structural information is available is the tetramerization domain, which forms a four-helix bundle with one alp[ha helix belonging to each p53 monomer. | The p53 protein consists of the N-terminal transactivation, the DNA binding or core, the tetramerization, and the C-terminal regulatory domain (Figure 3). This Proteopedia page discusses protein-DNA recognition by p53, thus focuses on the DBD of p53. The only other domain for which structural information is available is the tetramerization domain, which forms a four-helix bundle with one alp[ha helix belonging to each p53 monomer. | ||
The <scene name='Sandbox_Reserved_170/Complex/6'>DBD in tetrameric form binds to a response element</scene>, which consists of two half sites. These decameric half sites can be separated by a spacer of flexible length but in this case the spacer is of length zero base pairs. The<scene name='Sandbox_Reserved_170/Complex/7'>p53 tetramer binds DNA as a dimer of dimers</scene>. | The <scene name='Sandbox_Reserved_170/Complex/6'>DBD in tetrameric form binds to a response element</scene>, which consists of two half sites. These decameric half sites can be separated by a spacer of flexible length but in this case the spacer is of length zero base pairs. The <scene name='Sandbox_Reserved_170/Complex/7'>p53 tetramer binds DNA as a dimer of dimers</scene> with each dimer binding to one half site of the response element. | ||
<scene name='Sandbox_Reserved_170/Complex/5'> | The p53 DBD assumes an <scene name='Sandbox_Reserved_170/Complex/5'>immunoglobin fold</scene> | ||
<scene name='Sandbox_Reserved_170/Complex/8'>Zn ion</scene> | <scene name='Sandbox_Reserved_170/Complex/8'>Zn ion</scene> | ||
