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  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.

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 Creators:
Lupas, AN1, Author                 
Ferris, H1, Author           
Bassler, J1, Author           
Martin, J1, 2, Author                 
Schultz, J, Author
Dunin-Horkawicz, S1, Author                 
Hartmann, MD1, 3, Author                 
Coles, M1, 4, Author                 
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              

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 Abstract: 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].

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 Dates: 2018-12
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1007/s10863-018-9775-7
 Degree: -

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Title: International Conference BIOMEMBRANES 2018
Place of Event: Dolgoprudny, Russia
Start-/End Date: 2018-10-01 - 2018-10-05

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Title: Journal of Bioenergetics and Biomembranes
  Other : J. Bioenerg. Biomembr.
Source Genre: Journal
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Publ. Info: New York : Plenum Press.
Pages: - Volume / Issue: 50 (6) Sequence Number: - Start / End Page: 507 Identifier: ISSN: 0145-479X
CoNE: https://pure.mpg.de/cone/journals/resource/954925473404