Role of aromatic localization in the gating process of a potassium channel.
|Abstract||Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for transmembrane aromatic residues to reside at the interfaces. The process of aromatic localization is proposed as a means of directing and stabilizing st ... [truncated at 450 characters in length]|
|Author||Domene, Carmen; Vemparala, Satyavani; Klein, Michael L; et al|
|Subject||Biophysics Cell Membrane Computer Simulation G Protein-Coupled Inwardly-Rectifying Potassium Channels Ion Channel Gating Lipid Bilayers Lipids Models, Molecular Molecular Conformation Phenylalanine Potassium Channels Time Factors Tyrosine methods metabolism chemistry chemistry chemistry chemistry chemistry chemistry|
Activation segment exchange: a common mechanism of kinase autophosphorylation?
|Abstract||The crystal structure of the kinase domain from human checkpoint kinase 2 (Chk2) has shown, for the first time, the reciprocal exchange of activation segments between two adjacent molecules and provides the molecular basis for understanding the observed mode of Chk2 kinase activation via trans-autophosphorylation. With further examples of activation segment exchanged kinase domains now publicly available (i.e. Ste20-like kinase, Ser/Thr kinase 10 ... [truncated at 450 characters in length]|
|Author||Oliver, Antony W; Knapp, Stefan; Pearl, Laurence H;|
|Subject||Animals Crystallography, X-Ray Dimerization Humans Models, Biological Models, Chemical Molecular Conformation Phosphorylation Protein Conformation Protein Structure, Tertiary Protein-Serine-Threonine Kinases Serine Threonine methods chemistry metabolism physiology chemistry chemistry|
Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.
|Abstract||Acyl-CoA synthetases belong to the superfamily of adenylate-forming enzymes, and catalyze the two-step activation of fatty acids or carboxylate-containing xenobiotics. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Here, we report the first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/product/cofactor compl ... [truncated at 450 characters in length]|
|Author||Kochan, Grazyna; Pilka, Ewa S; von Delft, Frank; et al|
|Subject||Adenosine Monophosphate Adenosine Triphosphate Amino Acid Sequence Binding Sites Catalysis Coenzyme A Coenzyme A Ligases Crystallography, X-Ray Fatty Acids Humans Isoenzymes Models, Molecular Molecular Conformation Molecular Sequence Data Protein Conformation Sequence Alignment Substrate Specificity metabolism metabolism metabolism chemistry genetics metabolism chemistry metabolism chemistry genetics metabolism|