Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Replacement of a buried salt bridge by a hydrophobic cluster in the Arc repressor dimer sheds light on the role of ionic and hydrophobic interactions in proteins.
The structure of the catalytic domain of HIV integrase reveals a similarity with other proteins involved in DNA recombination or RNA degradation. Knowledge of the structure may help in the search for inhibitors of HIV replication.
A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.
Structural comparison identifies a similar basic fold for two enzymes which are involved in the phosphate-dependent formation or breakdown of oxygen-sugar linkages
