P53-DNA Recognition: Difference between revisions

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[[Image:p53-motif.jpg|thumb|right|300px|Figure 6: p53 binding site motif with G/C base pairs most conserved. PLoS has provided permission for usage of this figure.]]

Protein side chains and base pairs form direct contacts in the major groove among which the <scene name='Sandbox_Reserved_170/Arg280_contact/5'>contact between Arg280 and the guanine of the core element</scene> contributes most to binding specificity. This highly specific readout is due to the <scene name='Sandbox_Reserved_170/Arg280_contact/4'>bidentate hydrogen bond formed between Arg280 and guanine</scene>. As a result of this '''base readout''' ~~the identity of~~ the G/C base pairs in the CWWG core elements is the most conserved ~~position~~ in p53 response elements (Figure 5).

Protein side chains and base pairs form direct contacts in the major groove among which the <scene name='Sandbox_Reserved_170/Arg280_contact/5'>contact between Arg280 and the guanine of the core element</scene> contributes most to binding specificity. This highly specific readout is due to the <scene name='Sandbox_Reserved_170/Arg280_contact/4'>bidentate hydrogen bond formed between Arg280 and guanine</scene>. As a result of this '''base readout''' the G/C base pairs in the CWWG core elements are the most conserved positions in p53 response elements (Figure 5).

Another important contact is formed with the <scene name='Sandbox_Reserved_170/Lys_120/3'>Lys120 residue from the L1 loop of the protein</scene>. Lys120 is biologically very important because acetylation of this residue is known to trigger the apoptotic response of p53.

P53-DNA Recognition: Difference between revisions

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@@ Line 43: / Line 43: @@
 [[Image:p53-motif.jpg|thumb|right|300px|Figure 6: p53 binding site motif with G/C base pairs most conserved. PLoS has provided permission for usage of this figure.]]
-Protein side chains and base pairs form direct contacts in the major groove among which the <scene name='Sandbox_Reserved_170/Arg280_contact/5'>contact between Arg280 and the guanine of the core element</scene> contributes most to binding specificity. This highly specific readout is due to the <scene name='Sandbox_Reserved_170/Arg280_contact/4'>bidentate hydrogen bond formed between Arg280 and guanine</scene>. As a result of this '''base readout''' the identity of the G/C base pairs in the CWWG core elements is the most conserved position in p53 response elements (Figure 5).
+Protein side chains and base pairs form direct contacts in the major groove among which the <scene name='Sandbox_Reserved_170/Arg280_contact/5'>contact between Arg280 and the guanine of the core element</scene> contributes most to binding specificity. This highly specific readout is due to the <scene name='Sandbox_Reserved_170/Arg280_contact/4'>bidentate hydrogen bond formed between Arg280 and guanine</scene>. As a result of this '''base readout''' the G/C base pairs in the CWWG core elements are the most conserved positions in p53 response elements (Figure 5).
 Another important contact is formed with the <scene name='Sandbox_Reserved_170/Lys_120/3'>Lys120 residue from the L1 loop of the protein</scene>. Lys120 is biologically very important because acetylation of this residue is known to trigger the apoptotic response of p53.