Literature DB >> 10679469

Recognition of distorted DNA structures by HMG domains.

A Travers1.   

Abstract

Recent biochemical and structural studies have shown that the preferential recognition of distorted DNA structures, including DNA bulges, four-way junctions and cis-platinated DNA, by HMG domains is dependent on residues immediately preceding the second alpha helix of the L-shaped HMG domain.

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Year:  2000        PMID： 10679469     DOI： 10.1016/s0959-440x(99)00056-1

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  31 in total

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3.  HMG-D complexed to a bulge DNA: an NMR model.

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4.  The DNA architectural protein HMGB1 displays two distinct modes of action that promote enhanceosome assembly.

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5.  Ste11p, a high-mobility-group box DNA-binding protein, undergoes pheromone- and nutrient-regulated nuclear-cytoplasmic shuttling.

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Review 6.  Transcriptional activators and activation mechanisms.

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Review 7.  Origins of specificity in protein-DNA recognition.

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8.  Holliday junction-binding peptides inhibit distinct junction-processing enzymes.

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9.  Structure and dynamics of the DNA-binding protein HU of B. stearothermophilus investigated by Raman and ultraviolet-resonance Raman spectroscopy.

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10.  Crystallographic analysis of a sex-specific enhancer element: sequence-dependent DNA structure, hydration, and dynamics.

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