Key result
Open KcsA K+ channel reveals ~20 Å activation gate expansion that strains the bulge helices.
Why the study?
The structural mechanism of activation gating and its allosteric coupling to the selectivity filter in the full-length KcsA K+ channel was not fully understood.
Design
Structural, functional, and spectroscopic analysis of full-length KcsA channel mutant
Authors
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Structural details of open KcsA inform allosteric gating; leaves open translation to human cardiac channels or therapies.
Key points are not available for this paper at this time.
Uysal et al. (2011) studied this question. Structural analysis of the full-length KcsA K+ channel in the open conformation at 3.9 Å reveals that the activation gate expands about 20 Å, exerting strain on the bulge helices.
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