P53-DNA Recognition: Difference between revisions
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===Minor Groove Shape Readout=== | ===Minor Groove Shape Readout=== | ||
Most commonly, however, the residue Arg248 is found mutated in human tumors | Most commonly, however, the residue Arg248 is found mutated in human tumors. <scene name='Sandbox_Reserved_170/Arg248/2'>Arg248 contacts the minor groove</scene> although it does not usually form hydrogen bonds with the bases. Arg248 was shown to recognize regions of narrow minor groove associated with enhanced negative electrostatic potential ('''Figure 7''')<ref name='kitayner'/>. This observation provides a novel molecular explanation of the importance of Arg248 for p53-DNA binding and its role in cancer. The described mechanism known as '''shape readout''' was found to be broadly employed by arginine residues<ref name="nature">Rohs R, West SM, Sosinsky A, Liu P, Mann RS, Honig B. The role of DNA shape in protein-DNA recognition. Nature. 2009;461(7268):1248-53. [http://www.ncbi.nlm.nih.gov/pubmed/19865164 PMID:19865164].</ref>. | ||
==Hoogsteen vs. Watson-Crick Base Pair in p53 Binding Sites== | ==Hoogsteen vs. Watson-Crick Base Pair in p53 Binding Sites== |