9 Result(s)

Article

Dimers of DNA-PK create a stage for DNA double-strand break repair

DNA double-strand breaks are the most dangerous type of DNA damage and, if not repaired correctly, can lead to cancer. In humans, Ku70/80 recognizes DNA broken ends and recruits the DNA-dependent protein kinas...

Amanda K. Chaplin, Steven W. Hardwick… in Nature Structural & Molecular Biology (2021)

Article

Dissection of DNA double-strand-break repair using novel single-molecule forceps

Repairing DNA double-strand breaks (DSBs) by nonhomologous end joining (NHEJ) requires multiple proteins to recognize and bind DNA ends, process them for compatibility, and ligate them together. We constructed...

**g L. Wang, Camille Duboc, Qian Wu, Takashi Ochi… in Nature Structural & Molecular Biology (2018)

Article

Is one solution good enough?

Nicholas Furnham, Tom L Blundell, Mark A DePristo… in Nature Structural & Molecular Biology (2006)

Article

Crystal structure of an Xrcc4–DNA ligase IV complex

A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination. Here ...

Bancinyane L. Sibanda, Susan E. Critchlow, Jake Begun… in Nature Structural Biology (2001)

Article

Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding

Although ligand-induced receptor dimerization is a common prerequisite for receptor activation, the mode by which different growth factors bind their receptors and cause them to dimerize varies c...

Dimitri Y. Chirgadze, Jonathan P. Hepple, Hongjun Zhou… in Nature Structural Biology (1999)

Article

Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self–processing

The structure of L-aspartate-α-decarboxylase from E. coli has been determined at 2.2 Å resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded β-barrels capped...

Armando Albert, Venugopal Dhanaraj, Ulrich Genschel… in Nature Structural Biology (1998)

Article

Metalloproteinase super–families and drug design

The common topology of the matrix metalloproteinase family, and details of the structures of individual members, will intensify efforts to develop drugs for diseases such as arthritis and cancer.

Tom L Blundell in Nature Structural Biology (1994)