Potassium channel structures: do they conform?
|Abstract||Potassium channels are signalling elements vital to vertebrate neurotransmission, and cardiac and renal function. Two inherent qualities equip them for their role in the interconversion of chemical and electrical messages: high selectivity for potassium ions and the ability to open (gate) on cue. The crystal structure of KcsA, published in 1998, explained much about potassium selectivity and high ion flux. The enormous diversity of potassium chan ... [truncated at 450 characters in length]|
|Author||Gulbis, Jacqueline M; Doyle, Declan A;|
|Subject||Ion Channel Gating Ion Transport Ligands Models, Molecular Potassium Potassium Channels Protein Conformation Signal Transduction Structure-Activity Relationship physiology metabolism chemistry metabolism physiology|
The centaurin gamma-1 GTPase-like domain functions as an NTPase.
|Abstract||Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for C ... [truncated at 450 characters in length]|
|Author||Soundararajan, Meera; Yang, Xiaowen; Elkins, Jonathan M; et al|
|Subject||Amino Acid Sequence Binding Sites Cloning, Molecular Escherichia coli GTP-Binding Proteins GTPase-Activating Proteins Hydrolysis Models, Molecular Molecular Structure Nucleoside-Triphosphatase Nucleotides Protein Structure, Tertiary Signal Transduction Substrate Specificity ras Proteins metabolism chemistry metabolism chemistry metabolism chemistry metabolism metabolism chemistry metabolism|
Linear motif atlas for phosphorylation-dependent signaling.
|Abstract||Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding ... [truncated at 450 characters in length]|
|Author||Miller, Martin Lee; Jensen, Lars Juhl; Diella, Francesca; et al|
|Subject||14-3-3 Proteins Amino Acid Motifs Animals BRCA1 Protein Consensus Sequence Databases, Protein Humans Phosphorylation Phosphotransferases Phosphotyrosine Protein Binding Signal Transduction src Homology Domains chemistry chemistry chemistry metabolism|
UnPAKing the class differences among p21-activated kinases.
|Abstract||The p21-activated kinases (PAKs) are signal transducers, central to many vital cellular processes, including cell morphology, motility, survival, gene transcription and hormone signalling. The mammalian PAK family contains six serine/threonine kinases divided into two subgroups, group I (PAK 1-3) and group II (PAK4-6), based on their domain architecture and regulation. PAKs functioning as dynamic signalling nodes present themselves as attractive ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Soundararajan, Meera; Kumar, Rakesh; et al|
|Subject||Catalysis Signal Transduction Substrate Specificity p21-Activated Kinases metabolism|
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|