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|
Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.
|Abstract||Refsum disease (RD), a neurological syndrome characterized by adult onset retinitis pigmentosa, anosmia, sensory neuropathy, and phytanic acidaemia, is caused by elevated levels of phytanic acid. Many cases of RD are associated with mutations in phytanoyl-CoA 2-hydroxylase (PAHX), an Fe(II) and 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes the initial alpha-oxidation step in the degradation of phytenic acid in peroxisomes. We describe t ... [truncated at 450 characters in length]|
|Author||McDonough, Michael A; Kavanagh, Kathryn L; Butler, Danica; et al|
|Subject||Aspartic Acid Binding Sites Coenzyme A Crystallization Crystallography, X-Ray Cysteine Escherichia coli Ferrous Compounds Histidine Humans Ketoglutaric Acids Mixed Function Oxygenases Models, Molecular Mutation Peroxisomes Phytanic Acid Protein Binding Protein Structure, Secondary Recombinant Proteins Refsum Disease Structure-Activity Relationship Transfection metabolism genetics metabolism metabolism genetics metabolism metabolism metabolism chemistry genetics enzymology analogs and derivatives metabolism drug therapy enzymology|
Modeling of an ion channel in its open conformation.
|Abstract||We have modeled the structure of KirBac1.1 in an open state using as a starting point the structure of KirBac1.1 in its closed conformation (Protein Data Bank 1P7B). To test the validity of the open-state model, molecular dynamics simulations in octane, a lipid bilayer mimetic, were carried out. Simulations of the closed conformer were used for comparison purposes. The total simulation time was approximately 138 ns. The initial open model was ref ... [truncated at 450 characters in length]|
|Author||Domene, Carmen; Doyle, Declan A; Vénien-Bryan, Catherine;|
|Subject||Biophysics Burkholderia pseudomallei Crystallography, X-Ray Databases, Protein Glycine Models, Molecular Phenylalanine Potassium Potassium Channels, Inwardly Rectifying Protein Conformation Protein Structure, Secondary methods metabolism chemistry chemistry chemistry chemistry|
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|
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
|Abstract||Protein tyrosine phosphatases (PTPs) have key roles in a diverse range of cellular processes, and their dysregulation is associated with several human diseases. Many PTPs are recognized as potential drug targets; however, inhibitor development has focused only on a small number of enzymes, most notably PTP1B for type II diabetes and obesity, and MKP1 and CDC25 for cancer. The future challenge of selective-inhibitor development for PTPs will be si ... [truncated at 450 characters in length]|
|Author||Barr, Alastair J; Knapp, Stefan;|
|Subject||Animals Crystallography, X-Ray Drug Design Humans Mitogen-Activated Protein Kinase Kinases Models, Molecular Phosphorylation Protein Tyrosine Phosphatases chemistry metabolism physiology chemistry metabolism physiology|