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UID:DSC-14021
DTSTART;TZID=Europe/Berlin:20180316T130000
SEQUENCE:1521186325
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20180316T140000
URL:https://dresden-science-calendar.de/calendar/en/detail/14021
LOCATION:HZDR\, Bautzner Landstraße 40001328 Dresden
SUMMARY:Hoffmann: Institutskolloquium (FWP): \"Comparison of A1 and A2A ade
 nosine receptor dynamics  using FRET based receptor sensors\"
CLASS:PUBLIC
DESCRIPTION:Speaker: Prof. Dr. Carsten Hoffmann\nInstitute of Speaker: Inst
 itut für molekulare Zellbiologie\,CMB – Center for Molecular Biomedicin
 e\,Universitätsklinikum Jena\, Friedrich-Schiller-Universität Jena\nTopi
 cs:\nPhysik\n Location:\n  Name: HZDR (L9.3/216 - Bibliothek)\n  Street: B
 autzner Landstraße 400\n  City: 01328 Dresden\n  Phone: \n  Fax: \nDescri
 ption: Recently published crystal structures of the adenosine A2A receptor
  in the active and inactive state have revealed static endpoints of the co
 nformational changes associated with the activation process. To investigat
 e the activation dynamics of different adenosine receptor subtypes we used
  fluorescence resonance energy transfer (FRET) measurements of a modified 
 A1 and A2A receptor construct (A1R\, A2AR). Those optical probes where des
 igned by fusion of the cyan fluorescent protein (CFP) to the C-terminus of
  the receptor and insertion of the fluorescein arsenical hairpin binder (F
 lAsH) motif into the 3rd intracellular loop. Based on the ligand binding p
 ocket revealed from the crystal structure 10 optical probes including indi
 vidual mutations were created for each receptor. To compare A1R and A2AR d
 ynamics\, we established HEK293 cell lines stably expressing these optical
  probes and investigated the signal amplitude and the receptor activation 
 kinetics in living cells. We identified 3 different effects of these mutat
 ions. One class causes problems in membrane localization of the A1R but no
 t the A2AR. The 2nd group is involved in binding of the ribose moiety and 
 has stronger effects in the A1R compared to the A2AR. The 3rd class consis
 ts of the mutants that are involved in binding of the adenine moiety and h
 ave similar effects for adenosine and theophylline binding for the A2AR. T
 hus\, our study provides evidence that amino acids serve different functio
 ns within the A1R and A2AR ligand binding pocket. In summary the different
  signal amplitudes and different activation kinetics are indicative for a 
 different activation behavior of the A1R and A2AR and the data from the re
 ceptor mutants support these findings and gives new insight into the A1R- 
 structure.
DTSTAMP:20260904T065018Z
CREATED:20180123T074233Z
LAST-MODIFIED:20180316T074525Z
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