Could it be a member of a coiled coil at some point in its lifetime, as a
part of its function in regulating position or activity of this receptor?
Does the helix have sequence similarity to other coiled coils? see
https://www.uniprot.org/help/coiled for a primer on the topic.
Looks fun!
Emily.
Hi Michael,
Thanks for the information.
It is amphipathic. It follows a transmembrane helical domain of a cell
surface receptor and adopts an orientation parallel to the membrane. So it
may be associated with the membrane. I am just wondering if such
leucine-repeat motif is special among all amph
Dear Cheng,
Chris and Ruud have provided you with the typical interpretation of such a
motif, but you have forgotten to give the CCP4 community the context of this
leucine-repeat helix. Is it amphipathic? Does the protein also have
transmembrane helices (as suggested by the figure provided) w
