P53-DNA Recognition: Difference between revisions

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[[Image:p53-motif.jpg|thumb|right|300px|Figure 5: p53 binding site motif with G/C base pairs most conserved. PLoS has provided permission for usage of this figure<ref>Horvath MM, Wang X, Resnick MA, Bell DA. Divergent evolution of human p53 binding sites: cell cycle versus apoptosis. PLoS Genet. 2007 Jul;3(7):e127. [http://www.ncbi.nlm.nih.gov/pubmed/17677004 PMID:17677004].</ref>.]]
[[Image:p53-motif.jpg|thumb|right|300px|Figure 5: p53 binding site motif with G/C base pairs most conserved. PLoS has provided permission for usage of this figure<ref>Horvath MM, Wang X, Resnick MA, Bell DA. Divergent evolution of human p53 binding sites: cell cycle versus apoptosis. PLoS Genet. 2007 Jul;3(7):e127. [http://www.ncbi.nlm.nih.gov/pubmed/17677004 PMID:17677004].</ref>.]]


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''').
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 oldname='Sandbox_Reserved_170/Arg280_contact/4' name='P53-DNA_Recognition/P53_arg280_contact/1'>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 very important biologically because acetylation of this residue is known to trigger the apoptotic response of p53.
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 very important biologically because acetylation of this residue is known to trigger the apoptotic response of p53.

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Jaime Prilusky, Remo Rohs, Bailey Holmes, Ana Carolina Dantas Machado, Eran Hodis, Julia Tam, Masha Karelina, Sharon Kim, Skyler Saleebyan, Keziah Kim, Joseph M. Steinberger, Eric Martz, Alexander Berchansky, Michal Harel, Angel Herraez, Joel L. Sussman