Large T Antigen: Difference between revisions
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These rearrangements affect the position of <scene name='User:Udayan_Shevade/Sandbox1/Taghelicase_betahairpin/1'>the "β hairpin,"</scene> a positively-charged structure that protrudes into the central channel. ''Trans''-residues Arg498, Asp499 and Asp502 are located at the base of the hairpin, lending a lever-like functionality. The [http://www.sciencedirect.com/cache/MiamiImageURL/1-s2.0-S0092867404008906-gr7_lrg.jpg/0?wchp=dGLbVlk-zSkWb motion of the β hairpin] unwinds the DNA through the central channel <ref name='D'>PMID:15454080</ref>. | These rearrangements affect the position of <scene name='User:Udayan_Shevade/Sandbox1/Taghelicase_betahairpin/1'>the "β hairpin,"</scene> a positively-charged structure that protrudes into the central channel. ''Trans''-residues Arg498, Asp499 and Asp502 are located at the base of the hairpin, lending a lever-like functionality. The [http://www.sciencedirect.com/cache/MiamiImageURL/1-s2.0-S0092867404008906-gr7_lrg.jpg/0?wchp=dGLbVlk-zSkWb motion of the β hairpin] unwinds the DNA through the central channel <ref name='D'>PMID:15454080</ref>. | ||
[[Image:1SVM_L_O.jpg|500px|left|thumb]] | [[Image:1SVM_L_O.jpg|500px|left|thumb]] | ||
The helicase domain is also implicated in binding to p53, a transcription factor vital in tumor suppression. Binding of helicase inhibits the functional tetramerization of p53 on DNA<ref>PMID:1560412</ref>. | |||
