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 focusing on the DBD of p53. The only other domain for which structural information is available is the <scene name='Sandbox_Reserved_170/Tetra/2'>tetramerization domain</scene>, which forms as a dimer of dimers with one alpha helix and one beta strand contributed by 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 focusing on the DBD of p53. The only other domain for which structural information is available is the <scene name='Sandbox_Reserved_170/Tetra/2'>tetramerization domain</scene>, which forms as a dimer of dimers with one alpha helix and one beta strand contributed by each p53 monomer. | ||
<Structure load='3kz8bio-4mon.pdb.zip' size='400' frame='true' align='right' caption='Figure 5: Crystal structure of p53 DBD tetramer-DNA complex, [http://proteopedia.com/wiki/index.php/3kz8 PDB ID 3KZ8. | <Structure load='3kz8bio-4mon.pdb.zip' size='400' frame='true' align='right' caption='Figure 5: Crystal structure of p53 DBD tetramer-DNA complex, [http://proteopedia.com/wiki/index.php/3kz8 PDB ID 3KZ8].' scene='Sandbox_Reserved_170/Complex/6' /> | ||
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. | 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. | ||
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Another arginine residue, <scene name='Sandbox_Reserved_170/Arg273/2'>Arg273, contacts the phosphodiester backbone</scene> and seems to be important for human p53-DNA binding. Moreover, Arg273 is the second most common missense mutation in human cancer (Figure 2). | Another arginine residue, <scene name='Sandbox_Reserved_170/Arg273/2'>Arg273, contacts the phosphodiester backbone</scene> and seems to be important for human p53-DNA binding. Moreover, Arg273 is the second most common missense mutation in human cancer (Figure 2). | ||
[[Image:Kitayner-etal-Figure7.jpg|thumb|right|400px|Figure 7: DNA shape readout of narrow minor groove regions with enhanced electrostatic potential by Arg248 | [[Image:Kitayner-etal-Figure7.jpg|thumb|right|400px|Figure 7: DNA shape readout of narrow minor groove regions with enhanced electrostatic potential by Arg248. Nature Publishing Group has provided permission for usage of this figure<ref name='kitayner'/>.]] | ||
===Minor Groove Shape Readout=== | ===Minor Groove Shape Readout=== | ||
