P53-DNA Recognition: Difference between revisions

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The p53 DBD assumes the conformation of an <scene name='Sandbox_Reserved_170/Beta/1'>immunoglobulin-like fold consisting of a beta sandwich</scene>, which binds the response element in the major groove. A functionally important <scene name='Sandbox_Reserved_170/Zn/1'>Zn2+ ion coordinates the Cys176, His179, Cys238, Cys242 residues</scene> and, thus, stabilizes the fold of the DBD.
The p53 DBD assumes the conformation of an <scene name='Sandbox_Reserved_170/Beta/1'>immunoglobulin-like fold consisting of a beta sandwich</scene>, which binds the response element in the major groove. A functionally important <scene name='Sandbox_Reserved_170/Zn/1'>Zn2+ ion coordinates the Cys176, His179, Cys238, Cys242 residues</scene> and, thus, stabilizes the fold of the DBD.
<Structure load='P53tetra.pdb.zip' size='250' frame='true' align='left' caption='Figure 5: Crystal structure of p53 tetramerization domain, [http://proteopedia.com/wiki/index.php/1c26 PDB ID 1C26].' scene='Sandbox_Reserved_170/Tetra/2' />
The only other domain for which structural information is available is the ''tetramerization domain'' ['''Figure 5''', <scene name='Sandbox_Reserved_170/Tetra/2'>restore initial scene</scene>], which forms as a dimer of dimers with one alpha helix and one beta strand contributed by each p53 monomer. The tetramerization domain is ''not present'' in the crystal structure of the DBD (Figure 4).


===Protein-Protein Interactions===
===Protein-Protein Interactions===
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The reason for this deformation of the double helix is the <scene name='Group:USC-LCHS/3kz8_ba_hoogsteencloseup/2'>base pairing geometry in Hoogsteen base pairs</scene> with the approximately 180 degree rotation of adenine around the glycosidic bond and formation of hydrogen bonds with thymine at a different edge of the adenine base compared to <scene name='Group:USC-LCHS/3kmd_wcbp_closeup/1'>standard Watson-Crick base pairing</scene>, depicted here for the identical base pair in a p53 response element with different sequence from [[3kmd|PDB ID# 3KMD]].
The reason for this deformation of the double helix is the <scene name='Group:USC-LCHS/3kz8_ba_hoogsteencloseup/2'>base pairing geometry in Hoogsteen base pairs</scene> with the approximately 180 degree rotation of adenine around the glycosidic bond and formation of hydrogen bonds with thymine at a different edge of the adenine base compared to <scene name='Group:USC-LCHS/3kmd_wcbp_closeup/1'>standard Watson-Crick base pairing</scene>, depicted here for the identical base pair in a p53 response element with different sequence from [[3kmd|PDB ID# 3KMD]].
==Tetramerization Domain==
<Structure load='P53tetra.pdb.zip' size='250' frame='true' align='left' caption='Figure 5: Crystal structure of p53 tetramerization domain, [http://proteopedia.com/wiki/index.php/1c26 PDB ID 1C26].' scene='Sandbox_Reserved_170/Tetra/2' />
Aside from the DBD, the only other domain for which structural information is available is the ''tetramerization domain'' ['''Figure 5''', <scene name='Sandbox_Reserved_170/Tetra/2'>restore initial scene</scene>], which forms as a dimer of dimers with one alpha helix and one beta strand contributed by each p53 monomer. The tetramerization domain is ''not present'' in the crystal structure of the DBD (Figure 4).


=Further Reading=
=Further Reading=