Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

The bacterial aspartate receptor was reconstructed to eliminate the transmembrane domain, thus connecting the recognition domain directly to the effector domain. The resulting soluble receptor folded correctly and was no longer an integral membrane protein. Upon aspartate binding, this soluble receptor was stabilized to a similar extent as that of the native receptor. Of interest, this soluble receptor retained the ability to signal from the recognition to the effector domain. This result defines more clearly the role of the membrane and transmembrane domains in signal transduction and suggests that some ligand-induced motions in receptor proteins do not require the membrane or transmembrane domain for information transmission.

Bibliography

Ottemann, K. M., & Koshland, D. E. (1997). Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain. Proceedings of the National Academy of Sciences, 94(21), 11201–11204.

Authors 2
  1. Karen M. Ottemann (first)
  2. Daniel E. Koshland (additional)
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Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 10:31 a.m.)
Deposited 2 years, 4 months ago (April 22, 2023, 8:07 a.m.)
Indexed 1 year, 3 months ago (May 12, 2024, 11:02 p.m.)
Issued 27 years, 10 months ago (Oct. 14, 1997)
Published 27 years, 10 months ago (Oct. 14, 1997)
Published Online 27 years, 10 months ago (Oct. 14, 1997)
Published Print 27 years, 10 months ago (Oct. 14, 1997)
Funders 0

None

@article{Ottemann_1997, title={Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.21.11201}, DOI={10.1073/pnas.94.21.11201}, number={21}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Ottemann, Karen M. and Koshland, Daniel E.}, year={1997}, month=oct, pages={11201–11204} }