Using the proton-proton nuclear Overhauser effect, a large number (150) of interproton distances, both intra- and internucleotide, are determined in solution for a non-self-complementary DNA undecamer comprising a portion of the specific target site for the cAMP receptor protein in the gal operon. It is shown that these distances are very similar to those expected for classical B DNA (RMS difference of 0.5 A) but are significantly different from those expected for classical A DNA (RMS difference 1.1A). Glycosidic (chi) and C4'-C3' (delta) bond torsion angles are obtained by model building on the basis of the intranucleotide interproton distances. Whereas the sugar pucker exhibits little base-to-base variation with delta lying in the range 120 +/- 10 degrees, the glycosidic bond torsion angles of the pyrimidine and purine residues are significantly different, with chi pyr = -120 +/- 10 degrees and chi pur = -90 +/- 10 degrees.

Glycosidic bond

Dihedral angle

Z-DNA

10.1016/0014-5793(84)80582-7

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Citations (18)

Towards Atomic-Resolution Structure Determination of HIV-1 Capsid Assemblies using Magic Angle Spinning NMR

Biophysical Journal (2019)

Manman Lu Mingzhang Wang Jochem Struppe Werner Maas Angela M. Gronenborn

Heteronuclear molecule

Magic angle spinning

10.1016/j.bpj.2018.11.1682

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Citations (1)

Four-Dimensional Heteronuclear Triple-Resonance NMR Spectroscopy of Interleukin-1β in Solution

Science (1990)

Lewis E. Kay G. Marius Clore Ad Bax Angela M. Gronenborn

A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional carbon-13--nitrogen-15 (13C-15N)--edited nuclear Overhauser effect (NOE) spectroscopy to interleukin-1 beta, a protein of 153 residues. The NOEs between NH and aliphatic protons are first spread out into a third dimension by the 15N chemical shift of the amide 15N atom and subsequently into a fourth dimension by the 13C chemical shift of the directly bonded 13C atoms. By this means ambiguities in the assignment of NOEs between NH and aliphatic protons that are still present in the three-dimensional 15N-edited NOE spectrum due to extensive chemical shift overlap and degeneracy of aliphatic resonances are completely removed. Consequently, many more approximate interproton distance restraints can be obtained from the NOE data than was heretofore possible, thereby expanding the horizons of three-dimensional structure determination by NMR to larger proteins.

Heteronuclear molecule

10.1126/science.2377896

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Citations (308)

Three-Dimensional Solution Structure of Human Interleukin-4 by Multidimensional Heteronuclear Magnetic Resonance Spectroscopy

Science (1992)

Robert Powers Daniel S. Garrett Carl J. March Eric A. Frieden Angela M. Gronenborn

The three-dimensional solution structure of recombinant human interleukin-4, a protein of 133 residues and 15.4 kilodaltons that plays a key role in the immune and inflammatory systems, has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is dominated by a left-handed four-helix bundle with an unusual topology comprising two overhand connections. The linker elements between the helices are formed by either long loops, small helical turns, or short strands. The overall topology is remarkably similar to that of growth hormone and granulocyte-macrophage colony stimulating factor, despite the absence of any sequence homology, and substantial differences in the relative lengths of the helices, the length and nature of the various connecting elements, and the pattern of disulfide bridges. These three proteins, however, bind to cell surface receptors belonging to the same hematopoietic superfamily, which suggests that interleukin-4 may interact with its receptor in an analogous manner to that observed in the crystal structure of the growth hormone-extracellular receptor complex.

Heteronuclear molecule

Helix (gastropod)

Helix bundle

10.1126/science.256.5064.1673

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Citations (165)

The DNA-Binding Domain of GATA Transcription Factors—A Prototypical Type IV Cys2-Cys2 Zinc Finger

Springer eBooks (2005)

Angela M. Gronenborn

GATA transcription factor

LIM domain

GATA2