Crystal Structure of a Mammalian Voltage-Dependent Shaker 一个哺乳动物的电压依赖性振动的晶体结构.pptVIP

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2018-04-12 发布于江西
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Crystal Structure of a Mammalian Voltage-Dependent Shaker 一个哺乳动物的电压依赖性振动的晶体结构.ppt

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Crystal Structure of a Mammalian Voltage-Dependent Shaker 一个哺乳动物的电压依赖性振动的晶体结构.ppt

Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K+ Channel Stephen B. Long, Ernest B. Campbell, Roderick MacKinnon Review of K+ Channels in Neuronal Action Potentials Neurons are normally more permeable to K+ than Na+, leaving the resting membrane potential about –65mV. Synaptic or receptor potentials cause the voltage across the membrane to become more positive. If a specific threshold is reached, an action potential will occur,leaving the membrane more permeable to Na+ for a very short period. The membrane is depolarized and becomes more positive (+58mV) The voltage sensors of the K+ channels sense the change to a very positive membrane potential, and they become activated. The “inactivation peptide” that normally blocks the pore is released, and K+ ions move out of the cell in order to restore the resting membrane potential to –65mV. The Kv1.2 channel produces a sustained delayed rectifier current,which returns the membrane potential back to it’s resting potential soon after an action potential. These channels set the firing rate for action potentials because a consecutive one cannot be fired until the K+ channel has reset the membrane potential to it’s negative value. The Kv1.2 channel has 4 subunits that come together to form a single functional unit. Each subunit contains 6 transmembrane helices, and 2 connector helices (S1-T1, and S4-S5) S1-S4 helices from each subunit form the voltage sensor, and the S5 and S6 helices form the pore. S4 -S6 helices make up the selectivity filter of the inner pore. The Kv1.2 channel was co-expressed in yeast with the b2 K+ channel b subunit from a rat brain The proteins were crystallized by vapor diffusion, and then frozen in liquid nitrogen The resolution is 2.9A The electron density of the b and T1 subunits was strong (B factor= 59A2), these two domains are relatively immobile compared to the pore and voltage sensor-which was very mobile(B factor=162A2). Due to the weak electron density of the v