P53-DNA Recognition: Difference between revisions
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[[Image:p53-intro.jpg|thumb|left|300px|Figure 1: Crystal structure of a p53 DBD tetramer-DNA complex; [[3kz8|PDB ID# 3KZ8]]<ref name='kitayner'>Kitayner M, Rozenberg H, Rohs R, Suad O, Rabinovich D, Honig B, Shakked Z. Diversity in DNA recognition by p53 revealed by crystal structures with Hoogsteen base pairs. Nat Struct Mol Biol. 2010;17(4):423-9. [http://www.ncbi.nlm.nih.gov/pubmed/20364130 PMID:20364130].</ref>.]] | [[Image:p53-intro.jpg|thumb|left|300px|Figure 1: Crystal structure of a p53 DBD tetramer-DNA complex; [[3kz8|PDB ID# 3KZ8]]<ref name='kitayner'>Kitayner M, Rozenberg H, Rohs R, Suad O, Rabinovich D, Honig B, Shakked Z. Diversity in DNA recognition by p53 revealed by crystal structures with Hoogsteen base pairs. Nat Struct Mol Biol. 2010;17(4):423-9. [http://www.ncbi.nlm.nih.gov/pubmed/20364130 PMID:20364130].</ref>.]] | ||
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[[Image:consensus.jpg|thumb| | [[Image:consensus.jpg|thumb|left|250px|Figure 2: p53 consensus site; R= A or G, Y= C or T, and W=A or T.]] | ||
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[[Image:p53-domains.jpg|thumb| | [[Image:p53-domains.jpg|thumb|left|400px|Figure 3: Frequency of p53 mutants associated with cancer derived from [http://www-p53.iarc.fr/ IARC TP53 database]. Domain architecture; N-ter=N-terminal, DBD=DNA binding domain<ref name='kitayner'/>, Tet=Tetramerization<ref name='tetra'>Jeffrey PD, Gorina S, Pavletich NP. Crystal structure of the p53 tetramerization domain. Science 1995;267:1498-502. [http://www.ncbi.nlm.nih.gov/pubmed/7878469 PMID:7878469].</ref>, and C-ter=C-terminal domain. Intermediate regions are fairly disordered.]] | ||
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Also known as the '''Guardian of the Genome''', the tumor suppressor p53 is crucial in the natural defense against human cancer. The protein is activated by stress factors that can compromise the genomic integrity of the cell. This activation unleashes the function of p53 as a [[transcription factor]]. It binds as a tetramer ('''Figure 1''') to a large range of DNA response elements. The p53 consensus site ('''Figure 2''') is formed by two decameric half-sites, each containing a core element (red), that are separated by a variable number of base pairs (blue). | Also known as the '''Guardian of the Genome''', the tumor suppressor p53 is crucial in the natural defense against human cancer. The protein is activated by stress factors that can compromise the genomic integrity of the cell. This activation unleashes the function of p53 as a [[transcription factor]]. It binds as a tetramer ('''Figure 1''') to a large range of DNA response elements. The p53 consensus site ('''Figure 2''') is formed by two decameric half-sites, each containing a core element (red), that are separated by a variable number of base pairs (blue). | ||