Volume 8 Issue 6, June 2001

The LDL receptor plays a central role in the control of plasma cholesterol levels and the prevention of coronary artery disease. Recent studies now shed light on the structural organization of several independently folded modules and domains from which the receptor is assembled, providing substantial insights into the mechanics of receptor function and the consequences of disease causing mutations.

A mobile state of the kinesin–ADP head is discovered using multi- and single-molecule fluorescence polarization.

The crystal structure of Helicobacter pylori urease helps to explain how this enzyme contributes to bacterial survival in the acid environment of the human stomach.

The scope of structural genomics has recently been estimated by simulation of several target selection strategies based on the currently known protein sequence families. Useful characterization of most protein sequences will be possible by protein structure modeling, if structures of ∼16,000 carefully selected protein domains are determined experimentally. In the absence of globally coordinated target selection, three times as many structures may be required.

β-catenin functions both in cadherin-mediated cell adhesion and the Wnt signaling pathway. In these roles, β-catenin interacts with a multitude of protein partners including cadherins, α-catenin, axin, APC, and Tcf family transcription factors. Recent crystal structures show how β-catenin can achieve this remarkably diverse functionality.