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Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance.
A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a…
Regulation of MLL1 H3K4 methyltransferase activity by its core components
This study reports the first biochemical reconstitution of a functional four-component mixed-lineage leukemia protein-1 (MLL1) core complex and demonstrates that WDR5 mediates interactions of the MLL1 catalytic unit both with the common structural platform and with the histone substrate.
Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
The structure reveals the mechanistic basis for the recognition and catalytic excision of DNA damage by hOGG1 and by other members of the enzyme superfamily to which it belongs, and provides a rationale for the biochemical effects of inactivating mutations and polymorphisms in hogG1.
The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun
The interaction between the lymphoid-specific factor NFATp and the ubiquitous transcription factors Fos and Jun provides a novel mechanism for combinatorial regulation of interleukin-2 gene transcription, which integrates the calcium-dependent and the protein-kinase C-dependent pathways of T-cell activation.
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Hydrocarbon stapling of native peptides may provide a useful strategy for experimental and therapeutic modulation of protein-protein interactions in many signaling pathways.
A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA.
- P. Blainey, A. V. van Oijen, A. Banerjee, G. Verdine, X. Xie
- BiologyProceedings of the National Academy of Sciences…
- 11 April 2006
High-speed imaging of single hOgg1 enzyme molecules diffusing along DNA stretched by shear flow indicates that DNA glycosylases locate lesion bases by a massively redundant search in which the enzyme selectively binds 8-oxoguanine under kinetic control.
DNA (cytosine-5)-methyltransferases in mouse cells and tissues. Studies with a mechanism-based probe.
Data suggest that any sequence-specific de novo methylation mediated by Dnmt1 is either under the control of regulatory factors that interact with DnMT1, or is cued by alternative secondary structures in DNA.
Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
- J. Christopher Fromme, A. Banerjee, Susan J. Huang, G. Verdine
- Biology, ChemistryNature
- 12 February 2004
The use of disulphide crosslinking is reported to obtain high-resolution crystal structures of MutY–DNA lesion-recognition complexes that reveal the basis for recognizing both lesions in the A·oxoG pair and for catalysing removal of the adenine base.