Literature DB >> 3064080

The interaction of lac repressor headpiece with its operator: an NMR view.

R Boelens1, R M Lamerichs, J A Rullmann, J H van Boom, R Kaptein.   

Abstract

Analysis of nuclear Overhauser enhancements in two-dimensional NMR spectra of the complex of lac repressor headpiece with a 14 base pair lac operator fragment shows that the second helix of the headpiece binds in the major groove of DNA, as has been suggested. The orientation of this helix is approximately 180 degrees different from the proposed models and from that found in the X-ray structure of the 434 repressor-operator complex. The model of the lac headpiece-operator complex provides a good explanation for a large amount of biochemical, genetic and physical data.

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Year:  1988        PMID: 3064080

Source DB:  PubMed          Journal:  Protein Seq Data Anal        ISSN: 0931-9506


  3 in total

1.  The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study.

Authors:  R M Lamerichs; A Padilla; R Boelens; R Kaptein; G Ottleben; H Rüterjans; M Granger-Schnarr; P Oertel; M Schnarr
Journal:  Proc Natl Acad Sci U S A       Date:  1989-09       Impact factor: 11.205

2.  Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.

Authors:  S Morikawa; K Ogata; A Sekikawa; A Sarai; S Ishii; Y Nishimura; H Nakamura
Journal:  J Biomol NMR       Date:  1995-11       Impact factor: 2.835

3.  Identification of three residues in the basic regions of the bZIP proteins GCN4, C/EBP and TAF-1 that are involved in specific DNA binding.

Authors:  M Suckow; B von Wilcken-Bergmann; B Müller-Hill
Journal:  EMBO J       Date:  1993-03       Impact factor: 11.598

  3 in total

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