Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

 
 
DownloadE-Mail
  Axial helix rotation in transmembrane signal transduction

Lupas, A., Ferris, H., Bassler, J., Martin, J., Schultz, J., Dunin-Horkawicz, S., et al. (2018). Axial helix rotation in transmembrane signal transduction. Journal of Bioenergetics and Biomembranes, 50(6), 507.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Meeting Abstract

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Lupas, AN1, Autor                 
Ferris, H1, Autor           
Bassler, J1, Autor           
Martin, J1, 2, Autor                 
Schultz, J, Autor
Dunin-Horkawicz, S1, Autor                 
Hartmann, MD1, 3, Autor                 
Coles, M1, 4, Autor                 
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              
2Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477400              
3Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477392              
4Transmembrane Signal Transduction Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477410              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: The mechanism(s) by which extracelullar stimuli are transmitted from the
sensory domains of transmembrane receptors to the effector domains are
still substantially under debate. Whereas the most widespread model for
propagation of the stimulus is the piston model, in which the axial dis-
placement of one receptor subunit relative to the other activates the effec-
tor domain, we have put forward the cogwheel model (Fig. 1) [1], in
which axial rotation of the helices between two coiled-coil packing modes
[2] leads to the activation of the effector domain by a constrain-and-
release mechanism [3]. In this mechanism, the coiled-coil backbone of
the receptor sequesters the catalytic effector domains in an inactive con-
formation, until axial rotation of its helices releases the effector domains
to assume a catalytically productive conformation. We have recently
shown that this model applies not only to histidine kinases, but also to adenylyl cyclases [4].

Details

einblenden:
ausblenden:
Sprache(n):
 Datum: 2018-12
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1007/s10863-018-9775-7
 Art des Abschluß: -

Veranstaltung

einblenden:
ausblenden:
Titel: International Conference BIOMEMBRANES 2018
Veranstaltungsort: Dolgoprudny, Russia
Start-/Enddatum: 2018-10-01 - 2018-10-05

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Journal of Bioenergetics and Biomembranes
  Andere : J. Bioenerg. Biomembr.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: New York : Plenum Press.
Seiten: - Band / Heft: 50 (6) Artikelnummer: - Start- / Endseite: 507 Identifikator: ISSN: 0145-479X
CoNE: https://pure.mpg.de/cone/journals/resource/954925473404