WeightNameValue
1000 Titel
  • From Molecular Details of the Interplay between Transmembrane Helices of the Thyrotropin Receptor to General Aspects of Signal Transduction in Family A G-protein-coupled Receptors (GPCRs)
1000 Autor/in
  1. Kleinau, Gunnar |
  2. Hoyer, Inna |
  3. Kreuchwig, Annika |
  4. Haas, Ann-Karin |
  5. Rutz, Claudia |
  6. Furkert, Jens |
  7. Worth, Catherine L. |
  8. Krause, Gerd |
  9. Schülein, Ralf |
1000 Erscheinungsjahr 2011
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2011-05-17
1000 Erschienen in
1000 Quellenangabe
  • 286: 25859-25871
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3138303/ |
  • http://doi.org/10.1074/jbc.M110.196980 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • Transmembrane helices (TMHs) 5 and 6 are known to be important for signal transduction by G-protein-coupled receptors (GPCRs). Our aim was to characterize the interface between TMH5 and TMH6 of the thyrotropin receptor (TSHR) to gain molecular insights into aspects of signal transduction and regulation. A proline at TMH5 position 5.50 is highly conserved in family A GPCRs and causes a twist in the helix structure. Mutation of the TSHR-specific alanine (Ala-5935.50) at this position to proline resulted in a 20-fold reduction of cell surface expression. This indicates that TMH5 in the TSHR might have a conformation different from most other family A GPCRs by forming a regular α-helix. Furthermore, linking our own and previous data from directed mutagenesis with structural information led to suggestions of distinct pairs of interacting residues between TMH5 and TMH6 that are responsible for stabilizing either the basal or the active state. Our insights suggest that the inactive state conformation is constrained by a core set of polar interactions among TMHs 2, 3, 6, and 7 and in contrast that the active state conformation is stabilized mainly by non-polar interactions between TMHs 5 and 6. Our findings might be relevant for all family A GPCRs as supported by a statistical analysis of residue properties between the TMHs of a vast number of GPCR sequences.
1000 Sacherschließung
lokal G-protein-coupled Receptors (GPCR)
lokal Receptor Structure-Function
lokal Receptors
lokal Signal Transduction
lokal Thyroid
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/S2xlaW5hdSwgR3VubmFy|https://frl.publisso.de/adhoc/creator/SG95ZXIsIElubmE=|https://frl.publisso.de/adhoc/creator/S3JldWNod2lnLCBBbm5pa2E=|https://frl.publisso.de/adhoc/creator/SGFhcywgQW5uLUthcmlu|https://frl.publisso.de/adhoc/creator/UnV0eiwgQ2xhdWRpYQ==|https://frl.publisso.de/adhoc/creator/RnVya2VydCwgSmVucw==|https://frl.publisso.de/adhoc/creator/V29ydGgsIENhdGhlcmluZSBMLg==|https://frl.publisso.de/adhoc/creator/S3JhdXNlLCBHZXJk|https://frl.publisso.de/adhoc/creator/U2Now7xsZWluLCBSYWxm
1000 Förderer
  1. Deutsche Forschungsgemeinschaft |
1000 Fördernummer
  1. KR1273/4-1; KL2334/2-1
1000 Förderprogramm
  1. -
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft |
    1000 Förderprogramm -
    1000 Fördernummer KR1273/4-1; KL2334/2-1
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6403000.rdf
1000 Erstellt am 2017-06-13T10:13:01.705+0200
1000 Erstellt von 25
1000 beschreibt frl:6403000
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Wed May 16 12:34:39 CEST 2018
1000 Objekt bearb. Wed May 16 12:34:38 CEST 2018
1000 Vgl. frl:6403000
1000 Oai Id
  1. oai:frl.publisso.de:frl:6403000 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
1000 Gegenstand von

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