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• W2012318656 endingPage "771" @default.
• W2012318656 startingPage "769" @default.
• W2012318656 abstract "The transcription factor C/EBP uses a bipartite structural motif to bind DNA. Two protein chains dimerize through a set of amphipathic α helices termed the leucine zipper. Highly basic polypeptide regions emerge from the zipper to form a linked set of DNA contact surfaces. In the recently proposed a scissors grip model, the paired set of basic regions begin DNA contact at a central point and track in opposite directions along the major groove, forming a molecular clamp around DNA. This model predicts that C/EBP must undertake significant changes in protein conformation as it binds and releases DNA. The basic region of ligand-free C/EBP is highly sensitive to protease digestion. Pronounced resistance to proteolysis occurred when C/EBP associated with its specific DNA substrate. Sequencing of discrete proteolytic fragments showed that prominent sites for proteolysis occur at two junction points predicted by the scissors grip model. One junction corresponds to the cleft where the basic regions emerge from the leucine zipper. The other corresponds to a localized nonhelical segment that has been hypothesized to contain an N-cap and facilitate the sharp angulation necessary for the basic region to track continuously in the major groove of DNA." @default.
• W2012318656 created "2016-06-24" @default.
• W2012318656 creator A5030788201 @default.
• W2012318656 creator A5051143236 @default.
• W2012318656 creator A5060131568 @default.
• W2012318656 date "1990-08-17" @default.
• W2012318656 modified "2023-09-27" @default.
• W2012318656 title "Sequence-Specific DNA Binding by a Short Peptide Dimer" @default.
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• W2012318656 doi "https://doi.org/10.1126/science.2389142" @default.
• W2012318656 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2389142" @default.
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