Search results for "Allosteric interaction"

showing 2 items of 2 documents

Singular Location and Signaling Profile of Adenosine A2A-Cannabinoid CB1 Receptor Heteromers in the Dorsal Striatum

2018

The dorsal striatum is a key node for many neurobiological processes such as motor activity, cognitive functions, and affective processes. The proper functioning of striatal neurons relies critically on metabotropic receptors. Specifically, the main adenosine and endocannabinoid receptors present in the striatum, ie, adenosine A(2A) receptor (A(2A)R) and cannabinoid CB1 receptor (CB1R), are of pivotal importance in the control of neuronal excitability. Facilitatory and inhibitory functional interactions between striatal A(2A)R and CB1R have been reported, and evidence supports that this cross-talk may rely, at least in part, on the formation of A(2A)R-CB1R heteromeric complexes. However, th…

0301 basic medicineCannabinoid receptorAdenosineReceptor Adenosine A2Amedicine.medical_treatmentAdenosinaAdenosine A2A receptormediated inhibitionStriatumBiologyhuntingtons-disease micecannabinoid CB1Mice03 medical and health sciencesglutamatergic neurotransmission0302 clinical medicineReceptor Cannabinoid CB1NeurobiologyNeural PathwaysBasal gangliamedicineAnimalsHumansendocannabinoid systemGenetically modified animalProtein Structure QuaternaryA(2A) receptorsPharmacologyEndocannabinoid systemCorpus Striatumprotein-coupled receptorsProtein SubunitsPsychiatry and Mental healthtransgenic mouse modelHuntington Disease030104 developmental biologyMetabotropic receptornervous systembasal gangliaCannabinoidallosteric interactionsNeuroscience030217 neurology & neurosurgeryNeurobiologiaSignal Transduction
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Subunits composition and allosteric control in Carcinus aestuarii hemocyanin

1998

Carcinus aestuarii hemocyanin (Hc) exists in two aggregation forms at pH 7.5 and 20 mM Ca2+: 24S accounting for 90% of total hemocyanin and 16S accounting for 10%. Removal of metal cations by EDTA at neutral pH causes the complete dissociation of 24S hemocyanin into two different 16S. At pH 9.2, 24S hemocyanin dissociates into a pH stable 16S and a 5S component. The 5S component consists of three monomeric fractions named CaeSS1 (10%), CaeSS2 (50%) and CaeSS3 (40%); the latter fraction consisting of two isoforms. The fractions CaeSS1, CaeSS2 and CaeSS3 have been studied as far as their reassociation properties to form hexamers are concerned. We investigated the oxygen-binding properties of …

Protein ConformationStereochemistrymedicine.medical_treatmentProtein subunitAllosteric regulationHemocyaninBiochemistryAllosteric interactionchemistry.chemical_compoundProtein structureOxygen bindingAllosteric RegulationCrustaceaMetalloproteinsmedicineMetalloproteinAnimalschemistry.chemical_classificationHemocyanin; Oxygen binding; Allosteric interaction; OxygenbiologyHemocyaninHydrogen-Ion Concentrationbiology.organism_classificationOxygenCarcinus aestuariiMonomerBiochemistrychemistryHemocyaninsChromatography GelElectrophoresis Polyacrylamide GelOxygen bindingProtein Binding
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