Mechanism of corepressor-mediated specific DNA binding by the purine repressor

Article Abstract:

The corepressor-induced specific DNA-binding mechanism may be understood by studying the crystal structure of purine repressor. The purine repressor is bound to a corepressor and purF operator. A 2.2 angstrom resolution is needed for structural study of corepressor-free corepressor-binding domain of purine repressor. Unliganded subunits rotate open by about 23 degrees due to structural changes in the corepressor-binding pocket. This rotation causes disengagement of minor groove-binding hinge helices and repressor-DNA dissociation.

Analysis, DNA binding proteins

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RNA recognition: a family matter?

Article Abstract:

The study of proteins that bind to RNA has led to the identification of several protein families. Each family is characterized by a common sequence motif that is either known or supposed to interact directly with RNA. Current evidence suggests that the members of each family do not recognize similar RNA structures in the same way, and there is a need for more information on the detailed structure of RNA-protein complexes.

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"If the shoe fits": clues on structural recognition of DNA damage

Article Abstract:

Structural analysis of uracil-DNA glycosylase (UDG) reveals mechanisms for recognizing DNA damage. UDG is a 20-30 kDa polypeptide that acts on both single and double-stranded DNA. An active site that requires the uracil to become extrahelical is an interesting part of the DNA-binding mechanism.

Research, DNA damage

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