English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Meeting Abstract

Axial helix rotation in transmembrane signal transduction

MPS-Authors
/persons/resource/persons78342

Lupas,  AN       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons275634

Ferris,  H
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons272710

Bassler,  J
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons272291

Martin,  J       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons275270

Dunin-Horkawicz,  S       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons271510

Hartmann,  MD       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons271255

Coles,  M       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Transmembrane Signal Transduction Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-000D-0426-4
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].