Volume 10 Issue 3, March 2003

The high-resolution structure of the N-terminal half of an archaeal MCM protein domain sheds light on the enzyme's helicase activity and its role in DNA replication.

CREB phosphorylation is required for transcriptional activation, but how dephosphorylation couples with decreased transcription activity was less obvious. New findings indicate that CREB can recruit histone deacetylase HDAC1 and protein phosphatase 1 in a concerted action, thus leading to attenuated transcription.

Recent experiments have shown that the co-translational folding of the multi-domain LDL receptor in the endoplasmic reticulum does not occur in a vectorial manner. Instead, newly translated chains form misfolded states involving incorrect disulfide bonds between residues distant in sequence.

The structure of one of the two catalytic domains of angiotensin converting enzyme in complex with an inhibitor provides molecular insights into the substrate- and inhibitor-binding profiles of this clinically important enzyme.

The structure of the extracellular domain of HER2/ErbB2 reveals why the receptor is an orphan and provides valuable insight into the receptor's readiness to partner with other ErbB family members.