issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

June 2007 issue

Highlighted illustration

Cover illustration: DNA fragments of d(gcGAACgc) form a duplex, the adenosine residues bulging from which adopt two different conformations. One is folded back to interact with other part of the same duplex (blue) and the other is extended out to interact with the neighboring duplex (red), suggesting a molecular switch (p. 673).

research papers

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The crystal structure of human aldose reductase in complex with citrate at 0.82 Å resolution simultaneously shows the closed and open conformations of the safety belt. The two conformations correlate with different binding modes of the ligand.

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Two octamers with a sequence d(gcGAACgc) are associated to each other to form two types of bulge-containing duplexes different in conformation of the bulged-out adenosine residues, suggesting a molecular switch of the protruded adenosine residues.

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The X-ray structure of a parallel-stranded quadruplex has been solved to 1.5 Å resolution. The role of solvent molecules is analyzed.

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Inhibition of the TF–FVIIa complex is seen as a promising target that is key to the development of clinical candidates for various cardiovascular applications. The crystal structure of the TF–FVIIa enzyme complex has been analyzed in order to design and synthesize small-molecule inhibitors.

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The structure of the dual-specificity H1 phosphatase encoded by the smallpox virus has been determined and used to identify small-molecule inhibitors by in silico screening methods.

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Molecular-dynamics simulations of a small protein allowed an experimentally verifiable optimization of TLS-group selection.

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The crystal structure of the human complement protein CD59 is presented at 2.1 Å resolution. This structure is compared with a previous NMR model and the binding region for C8 and C9 is mapped.

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The 2.0 Å resolution crystal structure of hUBF HMG box5 has been solved using the single-wavelength anomalous-dispersion method, and the possible sites in hUBF HMG box5 which may interact with the first bromodomain in TAF1 were proposed.

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The structure of S. agalactiae family II inorganic pyrophosphatase in the presence of the competitive inhibitor imidodiphosphate was solved at 2.80 Å resolution by molecular replacement. Its structure is compared with those of other family II pyrophosphatases and structurally possible phosphorylation sites are discussed.

short communications

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The crystal structure of orotidine-5′-monophosphate decarboxylase, the C-terminal domain of human UMP synthase, was determined by molecular replacement using data from highly pseudo-merohedrally twinned monoclinic crystals with ac unit-cell parameters.

book reviews

Acta Cryst. (2007). D63, 750
doi: 10.1107/S0907444907013558
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