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Kainate receptors, which are glutamate activated excitatory neurotransmitter receptors, predominantly exist as heteromers of GluK2 and GluK5 subunits in the mammalian central nervous system. There are currently no structures of the full-length heteromeric kainate receptors. Here, we have used single molecule FRET to determine the specific arrangement of the GluK2 and GluK5 subunits within the dimer of dimers configuration in a full-length receptor. Additionally, we have also studied the dynamics and conformational heterogeneity of the amino-terminal and agonist-binding domain interfaces associated with the resting and desensitized states of the full-length heteromeric kainate receptor using FRET-based methods. The smFRET data are compared to similar experiments on the homomeric kainate receptor to provide insight into role of the differences in the conformational dynamics between the two to the functional differences. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.
This article was published in the following journal.
Name: Biochimica et biophysica acta. Biomembranes
Among the ionotropic glutamate receptors, the physiological role of kainate receptors is less well understood. Although ligands with selectivity towards the kainate receptor subtype GluK1 are availabl...
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New markers of viral activity are now under investigation. Aim of the study is to investigate the efficacy of new antiretroviral drugs by monitoring HIV-DNA dynamics in HIV-positive popula...
The study entitled " Asprosin Dynamics relating to serum Glucose levels under controlled alterations" investigates the dynamics of Asprosin in relation to glucose levels under controlled c...
This project aimed to optimize the therapeutic strategy for structural heart disease by choosing optimal treatment, such as,surgical treatment,interventional and surgery combined with inte...
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This is a short longitudinal preliminary study that aims to describe the dynamics of low-density subclinical malaria to support the final study design of a subsequent matched cohort study....
A group of AROMATIC HYDROCARBONS that have three rings joined as a triad around a single carbon atom so all three are conjoined, in contrast to a linear arrangement (ANTHRACENES) or angular arrangement (PHENANTHRENES).
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
A proteoglycan family (SLRPs) that is defined by a central domain which consists of a variable number of repeats of the motif LXXLxLXXNxL, where L may be LEUCINE; ISOLEUCINE; VALINE; or other hydrophobic amino acids. The N-terminal contains four conserved CYSTEINE residues and may be modified depending on function. SLRPs provide structural support to the EXTRACELLULAR MATRIX and are critical for regulating its assembly and dynamics at CELL-MATRIX JUNCTIONS.
A partnership, corporation, association, or other legal entity that enters into an arrangement for the provision of services with persons who are licensed to practice medicine, osteopathy, and dentistry, and with other care personnel. Under an IPA arrangement, licensed professional persons provide services through the entity in accordance with a mutually accepted compensation arrangement, while retaining their private practices. Services under the IPA are marketed through a prepaid health plan. (From Facts on File Dictionary of Health Care Management, 1988)
The erbB-2 gene is a proto-oncogene that codes for the erbB-2 receptor (RECEPTOR, ERBB-2), a protein with structural features similar to the epidermal growth factor receptor. Its name originates from the viral oncogene homolog (v-erbB) which is a truncated form of the chicken erbB gene found in the avian erythroblastosis virus. Overexpression and amplification of the gene is associated with a significant number of adenocarcinomas. The human c-erbB-2 gene is located at 17q21.2.