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• W2122583048 endingPage "708" @default.
• W2122583048 startingPage "697" @default.
• W2122583048 abstract "The study of the plant oncogene rolA has been hampered by a lack of structural information. Here we show that, despite a lack of significant sequence similarity to proteins of known structure, the rolA sequence adopts a known fold; that of the papillomavirus E2 DNA-binding domain. This fold is reliably identified by modern threading programs, which consider predicted secondary structure, but not by others. Although the rolA sequence is only around 16% identical to those of the available template structures, a structural model could be built that performed well against protein structure verification programs. The adopted strategy involved alignment corrections, justified by multiple model building and evaluation, with particular attention paid to the hydrophobic core residues. We find that rolA protein is predicted to resemble the template proteins in two key aspects; existence as a dimer and ability to bind DNA. rolA protein has recently been shown experimentally to possess DNA binding ability. This model predicts Lys 24 and Arg 27 to be involved in sequence-specific interactions and eight other residues to hydrogen-bond phosphate groups of the DNA." @default.
• W2122583048 created "2016-06-24" @default.
• W2122583048 creator A5009636964 @default.
• W2122583048 creator A5072004203 @default.
• W2122583048 date "1999-12-01" @default.
• W2122583048 modified "2023-10-17" @default.
• W2122583048 title "A structural model for therolA protein and its interaction with DNA" @default.
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• W2122583048 doi "https://doi.org/10.1002/(sici)1097-0134(19991201)37:4<697::aid-prot18>3.0.co;2-y" @default.
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• W2122583048 hasPublicationYear "1999" @default.
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