Volume 8 Issue 10, October 2001

Structures of two regions of BRCA1 offer important insights into the molecular properties of this tumor suppressor.

Death-associated protein kinase (DAP-kinase; DAPk) has been implicated in programmed cell death and tumor suppression. The recently solved crystal structure of the catalytic domain of human DAP-kinase reveals interesting 'fingerprint' regions that may be functionally important.

Recent crystal structures of error prone DNA polymerases that bypass damage in DNA templates provide counterexamples to high fidelity polymerases.

Crystal structures of the Escherichia coli DNA replication γ clamp loading complex and of a subunit of the clamp loader bound to a β clamp monomer provide a physical framework in which to view ATP-dependent modulation of γ complex–β interactions. The structural data suggest how the β ring is opened and loaded onto DNA in the absence of a direct interaction between the γ complex and the β dimer interface.