Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating

التفاصيل البيبلوغرافية
العنوان: Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating
المؤلفون: Xixi Chen, Richard W. Aldrich
المصدر: The Journal of General Physiology
بيانات النشر: The Rockefeller University Press, 2011.
سنة النشر: 2011
مصطلحات موضوعية: Membrane potential, BK channel, biology, Voltage-gated ion channel, Physiology, Chemistry, Inorganic chemistry, KcsA potassium channel, Ionic bonding, Gating, Article, Residue (chemistry), biology.protein, Biophysics, Humans, Large-Conductance Calcium-Activated Potassium Channels, Ion Channel Gating, Ion channel
الوصف: The pore-lining amino acids of ion channel proteins reside on the interface between a polar (the pore) and a nonpolar environment (the rest of the protein). The structural dynamics of this region, which physically controls ionic flow, are essential components of channel gating. Using large-conductance, Ca2+-dependent K+ (BK) channels, we devised a systematic charge–substitution method to probe conformational changes in the pore region during channel gating. We identified a deep-pore residue (314 in hSlo1) as a marker of structural dynamics. We manipulated the charge states of this residue by substituting amino acids with different valence and pKa, and by adjusting intracellular pH. We found that the charged states of the 314 residues stabilized an open state of the BK channel. With models based on known structures of related channels, we postulate a dynamic rearrangement of the deep-pore region during BK channel opening/closing, which involves a change of the degree of pore exposure for 314.
اللغة: English
تدمد: 1540-7748
0022-1295
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fba5a99021b02a063a8db43a893ba6eTest
http://europepmc.org/articles/PMC3149437Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....8fba5a99021b02a063a8db43a893ba6e
قاعدة البيانات: OpenAIRE