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• W2125318771 startingPage "1067" @default.
• W2125318771 abstract "The arginine-rich RNA binding motif is found in a wide variety of proteins, including several viral regulatory proteins. Although related at the primary sequence level, arginine-rich domains from different proteins adopt different conformations depending on the RNA site recognized, and in some cases fold only in the context of RNA. Here we show that the RNA binding domain of the Jembrana disease virus (JDV) Tat protein is able to recognize two different TAR RNA sites, from human and bovine immunodeficiency viruses (HIV and BIV, respectively), adopting different conformations in the two RNA contexts and using different amino acids for recognition. In addition to the conformational differences, the JDV domain requires the cyclin T1 protein for high-affinity binding to HIV TAR, but not to BIV TAR. The “chameleon-like” behavior of the JDV Tat RNA binding domain reinforces the concept that RNA molecules can provide structural scaffolds for protein folding, and suggests mechanisms for evolving distinct RNA binding specificities from a single multifunctional domain." @default.
• W2125318771 created "2016-06-24" @default.
• W2125318771 creator A5053156107 @default.
• W2125318771 creator A5074098242 @default.
• W2125318771 creator A5076764684 @default.
• W2125318771 date "2000-11-01" @default.
• W2125318771 modified "2023-10-16" @default.
• W2125318771 title "An RNA-Binding Chameleon" @default.
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• W2125318771 doi "https://doi.org/10.1016/s1097-2765(00)00105-2" @default.
• W2125318771 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11106746" @default.
• W2125318771 hasPublicationYear "2000" @default.
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