The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin
Abstract
Electrostatic interactions between charybdotoxin (CTX), a specific peptide pore blocker of K+ channels, and a Ca(2+)-activated K+ channel were investigated with a genetically manipulable recombinant CTX. Point mutations at certain charged residues showed only small effects on the binding affinity of the toxin molecule: Lys11, Glu12, Arg19, His21, Lys31, and Lys32. Replacement by Gln at Arg25, Lys27, or Lys34 strongly decreased the affinity of the toxin. These affinity changes were mainly due to large increases of toxin dissociation rates without much effect on association rates, as if close-range interactions between the toxin and its receptor site of the channel were disrupted. We also found that the neutralization of Lys27 to Gln removed the toxin's characteristic voltage dependence in dissociation rate. Mutation and functional mapping of charged residues revealed a molecular surface of CTX which makes direct contact with the extracellular mouth of the K+ channel.
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Citations
Cites
Price, M., Lee, S. C., & Deutsch, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.24.10171 · Cited by 183
Cited by
The charybdotoxin family of K+ channel-blocking peptides
Miller, C. (1995) · Neuron · doi:10.1016/0896-6273(95)90057-8 · Cited by 347
Self-citationGarcia-Calvo, M., Leonard, R. J., Novick, J., Stevens, S. P., Schmalhofer, W., Kaczorowski, G. J., & Garcia, M. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46707-x · Cited by 345
High-conductance calcium-activated potassium channels; Structure, pharmacology, and function
Kaczorowski, G. J., Knaus, H. G., Leonard, R. J., McManus, O. B., & Garcia, M. L. (1996) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110699 · Cited by 296
Metadata
- Authors
- Park, C. S., & Miller, C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1992-09-01
- Volume
- 31
- Issue
- 34
- Pages
- 7749-7755
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2069126258
- Cited by
- 158
- References
- 1
- FWCI
- 5.09
- Type
- journal article
- Language
- en
- Open access
- closed
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