The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif

  title={The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif},
  author={Jeffrey R. Huth and Carole A. Bewley and Mark S. Nissen and Jeremy N. S. Evans and Raymond Reeves and Angela M. Gronenborn and G. Marius Clore},
  journal={Nature Structural Biology},
The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51–90), and a DNA dodecamer containing the PRDII site of the interferon-β promoter has been solved by multidimensional nuclear magnetic resonance spectroscopy. The stoichiometry of the complex is one molecule of HMG-I(Y) to two molecules of DNA. The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating… 
Minor groove-binding architectural proteins: structure, function, and DNA recognition.
The structural features of these complexes and the roles they play in facilitating assembly of higher-order protein-DNA complexes are reviewed and elements that contribute to sequence-specific recognition and conformational changes are discussed.
Structure and function of the HMGI(Y) family of architectural transcription factors.
  • R. Reeves
  • Biology
    Environmental health perspectives
  • 2000
The levels of HMGI(Y) proteins in human cells have been proposed to be sensitive diagnostic indicators of both neoplastic transformation and metastatic progression and drugs based on the AT-hook motif offer the potential for development of new tumor therapeutic reagents.
Crystal Structure of a Complex of DNA with One AT-Hook of HMGA1
The structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)2, which has two potential AATT interacting groups found, is shown.
Protein Footprinting Reveals Specific Binding Modes of a High Mobility Group Protein I to DNAs of Different Conformation*
Large regions that flank the AT-hook motifs were found to be strongly protected against proteolysis in complexes with interferon-β promoter DNA, suggesting amino acid residues outside the AT -hooks considerably contribute to DNA binding.
Design and Characterization of a Short HMG‐I/DAT1 Peptide that Binds Specifically to the Minor Groove of DNA
This novel design HMG-1/DAT1 chimeric peptide possesses not only a high affinity to AT-rich DNA but also the sequence-specific binding in the minor groove of DNA, which may further lead to the design of short synthetic peptides for therapeutic applications.
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors
The three dimensional structure of the N-terminal domain (residues 1–42) of the copper-responsive transcription factor Amt1 from Candida glabrata has been determined by two-dimensional 1H-correlated
Crystal structure of an IRF‐DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences
The 2.2 Å resolution crystal structure of the DNA binding domain of one IRF‐2 bound to DNA is reported, and the ‘helix‐hairpin‐strand motif’ at the C terminus of the recognition helix is identified as a metal binding site that is commonly found in certain classes of DNA‐interactive proteins.
AT-hook peptides bind the major and minor groove of AT-rich DNA duplexes
The molecular models showed that 1:1 and 2:1 complex formation is driven by the capacity of the ATHPs to bind to the minor and major grooves of the AT-rich DNA oligomers, and complementary solution ITC results confirmed that the2:1 stoichiometry of ATHP: DNA is originated under native conditions in solution.


The solution structure of a specific GAGA factor–DNA complex reveals a modular binding mode
The structure of a complex between the DMA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic
Co-crystal structure of TBP recognizing the minor groove of a TATA element
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 Å
Multivalent DNA-binding properties of the HMG-1 proteins.
  • J. Maher, D. Nathans
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
It is demonstrated that high-affinity binding uses two or three appropriately spaced AT tracts as a single multivalent binding site, which has implications for binding to regulatory elements such as the interferon beta enhancer, TATA boxes, and serum response elements.
Structural basis for DNA bending by the architectural transcription factor LEF-1
The solution structure of a complex of the LEF-1 H MG domain and adjacent basic region with its cognate DNA is reported, revealing the HMG domain bound in the widened minor groove of a markedly distorted and bent double helix.
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.
The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has
Short peptide fragments derived from HMG-I/Y proteins bind specifically to the minor groove of DNA.
Using NMR spectroscopy, the DNA binding of SPRKSPRK is investigated, which is one such A,T-specific motif, and the peptide PKGKP does not interact with the same oligonucleotide duplexes, indicating that the arginine guanidinium groups are major determinants of the A, T specificity.