Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1995 Dec;69(6):2415–2418. doi: 10.1016/S0006-3495(95)80111-6

A random flight chain model for the tether of the Shaker K+ channel inactivation domain.

L C Timpe 1, L Peller 1
PMCID: PMC1236479  PMID: 8599648

Abstract

Rapid inactivation of Shaker K+ channels occurs when a domain in the amino terminal region of the channel protein blocks the pore. Some part of the sequence between the inactivating domain and the first transmembrane segment may form a flexible tether. We consider the possibility that the tether has no secondary structure, but is rather a polypeptide random coil. The local concentration of the tethered inactivation domain and the dependence of the inactivation rate on chain length can then be calculated by using the Jacobson-Stockmayer equation. A chain of 30-100 amino acids is consistent with the sensitivity of the inactivation rate to chain length mutations.

Full text

PDF
2415

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Crothers D. M., Metzger H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry. 1972 Mar;9(3):341–357. doi: 10.1016/0019-2791(72)90097-3. [DOI] [PubMed] [Google Scholar]
  2. Demo S. D., Yellen G. The inactivation gate of the Shaker K+ channel behaves like an open-channel blocker. Neuron. 1991 Nov;7(5):743–753. doi: 10.1016/0896-6273(91)90277-7. [DOI] [PubMed] [Google Scholar]
  3. Hoshi T., Zagotta W. N., Aldrich R. W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 1990 Oct 26;250(4980):533–538. doi: 10.1126/science.2122519. [DOI] [PubMed] [Google Scholar]
  4. Jencks W. P. On the attribution and additivity of binding energies. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4046–4050. doi: 10.1073/pnas.78.7.4046. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Li M., Jan Y. N., Jan L. Y. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science. 1992 Aug 28;257(5074):1225–1230. doi: 10.1126/science.1519059. [DOI] [PubMed] [Google Scholar]
  6. Liebovitch L. S., Selector L. Y., Kline R. P. Statistical properties predicted by the ball and chain model of channel inactivation. Biophys J. 1992 Dec;63(6):1579–1585. doi: 10.1016/S0006-3495(92)81732-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. MacKinnon R., Aldrich R. W., Lee A. W. Functional stoichiometry of Shaker potassium channel inactivation. Science. 1993 Oct 29;262(5134):757–759. doi: 10.1126/science.7694359. [DOI] [PubMed] [Google Scholar]
  8. MacKinnon R. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 1991 Mar 21;350(6315):232–235. doi: 10.1038/350232a0. [DOI] [PubMed] [Google Scholar]
  9. Murrell-Lagnado R. D., Aldrich R. W. Energetics of Shaker K channels block by inactivation peptides. J Gen Physiol. 1993 Dec;102(6):977–1003. doi: 10.1085/jgp.102.6.977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Murrell-Lagnado R. D., Aldrich R. W. Interactions of amino terminal domains of Shaker K channels with a pore blocking site studied with synthetic peptides. J Gen Physiol. 1993 Dec;102(6):949–975. doi: 10.1085/jgp.102.6.949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Schwarz T. L., Tempel B. L., Papazian D. M., Jan Y. N., Jan L. Y. Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. Nature. 1988 Jan 14;331(6152):137–142. doi: 10.1038/331137a0. [DOI] [PubMed] [Google Scholar]
  12. Wang J. C., Davidson N. On the probability of ring closure of lambda DNA. J Mol Biol. 1966 Aug;19(2):469–482. doi: 10.1016/s0022-2836(66)80017-7. [DOI] [PubMed] [Google Scholar]
  13. Zagotta W. N., Hoshi T., Aldrich R. W. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science. 1990 Oct 26;250(4980):568–571. doi: 10.1126/science.2122520. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES