Voltage gated potassium ion channel has been studied extensively 电压门控钾离子通道已被广泛的的研究.docVIP

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Voltage gated potassium ion channel has been studied extensively 电压门控钾离子通道已被广泛的的研究.doc

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Voltage gated potassium ion channel has been studied extensively 电压门控钾离子通道已被广泛的的研究

Andinet Amare Biophysics 490 April 20, 2003 Comparison of Potassium and Mechanosensitive ion Channels Introduction Voltage gated potassium ion channel has been studied extensively by physiological means. Electro-physiological, mutation, fluorescence anisotropy and fluorescence energy transfer studies contribute to the wealth of information available on this system, particularly how the channel senses potential difference and respond to it. Missing from our knowledge is the structure of the system. The crystal structure of the channel does not exist to date. Voltage gated potassium ion channel, Kv, demonstrates a large sequence similarity with other potassium channels and distant similarity to sodium and calcium ion channels (Doyle et al). The bacterial potassium ion channel, (KcsA) first crystallized in 1998 by Doyle et al, has been important in guiding our understanding of the Kv structure. Studies with neurotoxins establish structural similarities of these two channels. Bass et al. recently reported the crystal structure of a small conductance mechano-sensitive ion channel (MscS). This channel responds to osmotic pressure and shows small voltage dependant gating. The potential of this structure to complement and extend our understanding of voltage-gated channels is immense. This paper compares the structures of K+ and small mechano-sensitive ion channels to each other, and relate them to empirical knowledge of voltage gated K+ channel. Sequence and general structural notes The potassium ion channel that will be discussed in this paper is isolated from bacterium Streptomyces lividans (Doyle et al.), and will be referred to as KcsA. The structure, listed in the Protein Data Bank as 1BL8, is resolved to 3.2A for positions 23 to 119. The first 23 amino-acids and the cytoplasmic carboxyl terminus (126 to 158) are missing from the structure. KcsA is a tetramer with four fold symmetry. Each subunit is made of two transmembrane alpha helices, additional he