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Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland
Correspondence: Address reprint requests to H. Robert Guy, Laboratory of Experimental and Computational Biology, National Cancer Institute, National Institutes of Health, 12 South Dr., Bethesda, MD 20892-5567. Tel.: 301-496-2068; Fax: 301-402-4724; E-mail: bg4y{at}nih.gov.
In the preceding, accompanying article, we present models of the structure and voltage-dependent gating mechanism of the KvAP bacterial K+ channel that are based on three types of evidence: crystal structures of portions of the KvAP protein, theoretical modeling criteria for membrane proteins, and biophysical studies of the properties of native and mutated voltage-gated channels. Most of the latter experiments were performed on the Shaker K+ channel. Some of these data are difficult to relate directly to models of the KvAP channel's structure due to differences in the Shaker and KvAP sequences. We have dealt with this problem by developing new models of the structure and gating mechanism of the transmembrane and extracellular portions of the Shaker channel. These models are consistent with almost all of the biophysical data. In contrast, much of the experimental data are incompatible with the "paddle" model of gating that was proposed when the KvAP crystal structures were first published. The general folding pattern and gating mechanisms of our current models are similar to some of our earlier models of the Shaker channel.
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