The x-ray structure of the unactivated kinase domain of insulin-like growth factor-1 receptor (IGFRK-0P) is reported here at 2.7 Å resolution. IGFRK-0P is composed of two lobes connected by a hinge ...region. The N-terminal lobe of the kinase is a twisted β-sheet flanked by a single helix, and the C-terminal lobe comprises eight α-helices and four short β-strands. The ATP binding pocket and the catalytic center reside at the interface of the two lobes. Despite the overall similarity to other receptor tyrosine kinases, three notable conformational modifications are observed: 1) this kinase adopts a more closed structure, with its two lobes rotated further toward each other; 2) the conformation of the proximal end of the activation loop (residues 1121–1129) is different; 3) the orientation of the nucleotide-binding loop is altered. Collectively, these alterations lead to a different ATP-binding pocket that might impact on inhibitor designs for IGFRK-0P. Two molecules of IGFRK-0P are seen in the asymmetric unit; they are associated as a dimer with their ATP binding clefts facing each other. The ordered N terminus of one monomer approaches the active site of the other, suggesting that the juxtamembrane region of one molecule could come into close proximity to the active site of the other.
We report on Czochralski growth, structure, spectroscopy and laser operation of tetragonal disordered calcium aluminate crystals, Tm, Ho:Ca(Gd, Lu)AlO 4 . The laser generates 763 mW at 2078.6 nm with ...a slope efficiency of 26.4% (tuning range: 212 nm).
Analysis of nosocomial Staphylococcus haemolyticus by MLST and MALDI-TOF mass spectrometry Kornienko, Maria; Elena IlinaauthorFederal Research and Clinical Centre of PhysicalâChemical Medicine, Moscow, Russia; Ludmila LubasovskayaauthorFederal State Budget Institution Research Center for Obstetrics, Gynecology and Perinatology, Moscow, Russia ...
2015
Journal Article
PDF