Andrew P. Seddon

TL;DR: The structure of human PCSK9 shows the subtilisin-like catalytic site blocked by the prodomain in a noncovalent complex and inaccessible to exogenous ligands, and that the C-terminal domain has a novel fold.

TL;DR: The structure of CETP is described, revealing a 60-Å-long tunnel filled with two hydrophobic cholesteryl esters and plugged by an amphiphilic phosphatidylcholine at each end, suggesting that neutral lipids pass through this continuous tunnel.

TL;DR: The first crystal structure of a herpesvirus polymerase is presented, the Herpes Simplex Virus type 1 DNA polymerase, at 2.7 Å resolution and a novel inhibition mechanism is proposed in which a representative of a series of non-nucleosidic viral polymerase inhibitors, the 4-oxo-dihydroquinolines, binds at the polymerase active site interacting non-covalently with both the polymer enzyme and the DNA duplex.

TL;DR: A novel mechanism to explain the functional interaction of FGF-2 with heparin and its transmembrane receptor is proposed.

TL;DR: Three-dimensional crystal structures of human cathepsin S in complex with potent covalent inhibitors, the aldehyde inhibitor 4-morpholinecarbonyl-Phe-(S-benzyl)Cys-Psi(CH=O), and the vinyl sulfone irreversible inhibitors 4- morpholinecarbonol-Leu-Hph-PsI(CH-SO(2)-phenyl) are determined.