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|
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|
Protein-protein interaction site mapping using NMR-detected mutational scanning.
|Abstract||We demonstrate a novel NMR method for the mapping of protein-protein interaction sites. In our approach protein-protein binding sites are mapped by competition binding experiments using indirect NMR reporter technology and Ala positional scanning. The methodology provides high sensitivity, ease of implementation and high-throughput capabilities. The feasibility of the technique is demonstrated with an application to the beta-Catenin/Tcf4 complex.|
|Author||Baminger, Bettina; Ludwiczek, Martin L; Kontaxis, Georg; et al|
|Subject||Binding, Competitive Humans Ligands Models, Molecular Mutation Nuclear Magnetic Resonance, Biomolecular Protein Interaction Mapping Reproducibility of Results TCF Transcription Factors Transcription Factor 7-Like 2 Protein beta Catenin genetics methods methods metabolism metabolism|
Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms.
|Abstract||All eukaryotic cellular mRNAs contain a 5' m(7)GpppN cap. In addition to conferring stability to the mRNA, the cap is required for pre-mRNA splicing, nuclear export and translation by providing an anchor point for protein binding. In translation, the interaction between the cap and the eukaryotic initiation factor 4E (eIF4E) is important in the recruitment of the mRNAs to the ribosome. Human 4EHP (h4EHP) is a homologue of eIF4E. Like eIF4E it is ... [truncated at 450 characters in length]|
|Author||Rosettani, Pamela; Knapp, Stefan; Vismara, Maria-Grazia; et al|
|Subject||Amino Acid Sequence Binding Sites Calorimetry Conserved Sequence Crystallography, X-Ray Eukaryotic Initiation Factor-4E Evolution, Molecular Guanosine Triphosphate Humans Models, Molecular Molecular Sequence Data Mutation Peptides Protein Binding RNA Cap-Binding Proteins RNA Caps chemistry genetics metabolism chemistry metabolism chemistry chemistry genetics metabolism chemistry|
Out of the box binding determines specificity of SH2 domain interaction.
|Abstract||SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence specificities. A recent structure by Bae et al. revealed that SH2 domain specificity can be mediated by secondary binding sites located outside the phosphotyrosine binding pocket.|
|Author||Müller, Susanne; Knapp, Stefan;|
|Subject||Binding Sites Mutation Phosphotyrosine Protein Binding Signal Transduction src Homology Domains genetics chemistry genetics metabolism|