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Structure of the ligand‐binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist
Oestrogens exert their physiological effects through two receptor subtypes. Here we report the three‐dimensional structure of the oestrogen receptor beta isoform (ERβ) ligand‐binding domain (LBD) in… Expand
A serine protease triad forms the catalytic centre of a triacylglycerol lipase
TRUE Upases attack triacylglycerols and act at an oil–water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far… Expand
Structural insights into the mode of action of a pure antiestrogen.
BACKGROUND Estrogens exert their effects on target tissues by binding to a nuclear transcription factor termed the estrogen receptor (ER). Previous structural studies have demonstrated that each… Expand
How insulin engages its primary binding site on the insulin receptor
Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival. Insulin resistance contributes to the pathogenesis… Expand
A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
LIPASES are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl… Expand
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution
- V. Ducros, A. Brzozowski, +6 authors G. Davies
- Chemistry, Medicine
- Nature Structural Biology
- 1 April 1998
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue… Expand
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
The three-dimensional structure of the Bacillus stearothermophilus "maltogenic" alpha-amylase, Novamyl, has been determined by X-ray crystallography at a resolution of 1.7 A. Unlike conventional… Expand
Clear strategy screens for macromolecular crystallization
The development of high-throughput crystallography combined with the wealth of already accumulated information about protein crystallization properties requires constant revision of current… Expand
Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.
The already known X-ray structures of lipases provide little evidence about initial, discrete structural steps occurring in the first phases of their activation in the presence of lipids (process… Expand
Structural characterization of human heparanase reveals insights into substrate recognition
- Liang Wu, C. Viola, A. Brzozowski, G. Davies
- Medicine, Chemistry
- Nature Structural &Molecular Biology
- 16 November 2015
Heparan sulfate (HS) is a glycosaminoglycan that forms a key component of the extracellular matrix (ECM). Breakdown of HS is carried out by heparanase (HPSE), an endo-β-glucuronidase of the glycoside… Expand