The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
|Abstract||The receptor-type protein tyrosine phosphatases (RPTPs) are integral membrane proteins composed of extracellular adhesion molecule-like domains, a single transmembrane domain, and a cytoplasmic domain. The cytoplasmic domain consists of tandem PTP domains, of which the D1 domain is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined the crystal structur ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Debreczeni, Judit E; Longman, Emma; et al|
|Subject||Amino Acid Sequence Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Tertiary Protein Tyrosine Phosphatases Receptor-Like Protein Tyrosine Phosphatases, Class 2 Sequence Homology, Amino Acid Solutions Structural Homology, Protein chemistry metabolism|
Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution.
|Author||Barr, Alastair J; Debreczeni, Judit E; Eswaran, Jeyanthy; et al|
|Subject||Amino Acid Sequence Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Mutation Protein Structure, Tertiary Protein Tyrosine Phosphatase, Non-Receptor Type 1 Protein Tyrosine Phosphatases Protein Tyrosine Phosphatases, Non-Receptor Sequence Alignment Structural Homology, Protein genetics chemistry genetics metabolism|
Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.
|Abstract||To this day, a significant proportion of the human genome remains devoid of functional characterization. In this study, we present evidence that the previously functionally uncharacterized product of the human DHRS10 gene is endowed with 17beta-HSD (17beta-hydroxysteroid dehydrogenase) activity. 17beta-HSD enzymes are primarily involved in the metabolism of steroids at the C-17 position and also of other substrates such as fatty acids, prostaglan ... [truncated at 450 characters in length]|
|Author||Lukacik, Petra; Keller, Brigitte; Bunkoczi, Gabor; et al|
|Subject||17-Hydroxysteroid Dehydrogenases Amino Acid Sequence Binding Sites Cell Line Crystallography, X-Ray Cytosol Gene Expression Humans Kinetics Ligands Models, Molecular Molecular Sequence Data NAD Organ Specificity Oxidation-Reduction Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Structural Homology, Protein chemistry genetics isolation and purification metabolism enzymology metabolism|
Structure-activity relationships of human AKR-type oxidoreductases involved in bile acid synthesis: AKR1D1 and AKR1C4.
|Abstract||Two members of the human aldo-keto reductase (AKR) superfamily participate in the biosynthesis of bile acids by catalyzing the NADP(H) dependent reduction of 3-keto groups (AKR1C4) and Delta4 double bonds (AKR1D1) of oxysterol precursors. Structure determination of human AKR1C4 and homology modelling of AKR1D1 followed by docking experiments were used to explore active site geometries. Substrate docking resulted in ligand poses satisfying catalyt ... [truncated at 450 characters in length]|
|Author||Lee, Wen Hwa; Lukacik, Petra; Guo, Kunde; et al|
|Subject||Bile Acids and Salts Catalytic Domain Crystallography, X-Ray Humans Ligands Models, Molecular Oxidoreductases Structural Homology, Protein Structure-Activity Relationship Tryptophan biosynthesis chemistry metabolism metabolism|
SGC--structural biology and human health: a new approach to publishing structural biology results.
|Author||Lee, Wen Hwa; Atienza-Herrero, Julián; Abagyan, Ruben; et al|
|Subject||Amino Acid Sequence Computational Biology Databases, Protein Genomics Humans Protein Conformation Protein Folding Proteins Publishing Structural Homology, Protein economics methods chemistry classification genetics|