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The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling. In its active conformation, the SH2 domain tightly interacts with the...
General transcription factor TFIID consists of TATA box-binding protein (TBP) and TBP-associated factors (TAF II s), which together playa central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAF II (dTAF II 230) binds directly to TBP and inhibits TBP binding to the TATA box. We report here the...
The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage λ and boxB RNA was determined by heteronuclear magnetic resonance spectroscopy. A bent α helix in N recognizes primarily the shape and negatively charged surface of the boxB hairpin through multiple hydrophobic and ionic interactions. The GAAGA boxB loop forms a GNRA fold, previously...
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