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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Stanfield P R, Davies N W, Shelton P A, Sutcliffe M J, Khan I A, Brammar W J, Conley E C

Department of Cell Physiology and Pharmacology, University of Leicester.

J Physiol. 1994 Jul 1;478 ( Pt 1)(Pt 1):1-6. doi: 10.1113/jphysiol.1994.sp020225.

We describe the effects on channel function of changing an aspartate residue (Asp172) in a membrane-spanning alpha-helix of the murine inward rectifier, IRK1, by site-directed mutagenesis. 2. Alteration of Asp172 to Glu (charged) or to Gln or Asn (polar but uncharged) produced functional channels showing inward rectification, though rectification was weaker with Gln and Asn. 3. Intrinsic gating around the potassium equilibrium potential, EK, was conserved only if the charge on residue 172 was conserved. Currents through channels with Gln or Asn in this position showed no time dependence under hyperpolarization. 4. The change from Asp to Gln also reduced the affinity for internal Mg2+ at least fivefold, indicating that Asp172 also forms part of the site for Mg2+ blockage. 5. The consequences for channel structure of Asp172 lining the pore are discussed.

我们通过定点诱变描述了改变小鼠内向整流钾通道IRK1跨膜α螺旋中天冬氨酸残基（Asp172）对通道功能的影响。2. 将Asp172替换为Glu（带电荷）、Gln或Asn（极性但不带电荷）产生了具有内向整流特性的功能性通道，不过Gln和Asn的整流作用较弱。3. 只有当172位残基的电荷保持不变时，围绕钾平衡电位EK的内在门控才得以保留。在超极化情况下，该位置为Gln或Asn的通道的电流没有时间依赖性。4. 从Asp变为Gln也使对内部Mg2+的亲和力至少降低了五倍，表明Asp172也是Mg2+阻断位点的一部分。5. 讨论了位于孔道内的Asp172对通道结构的影响。

Stanfield P R, Davies N W, Shelton P A, Sutcliffe M J, Khan I A, Brammar W J, Conley E C

Department of Cell Physiology and Pharmacology, University of Leicester.

J Physiol. 1994 Jul 1;478 ( Pt 1)(Pt 1):1-6. doi: 10.1113/jphysiol.1994.sp020225.

We describe the effects on channel function of changing an aspartate residue (Asp172) in a membrane-spanning alpha-helix of the murine inward rectifier, IRK1, by site-directed mutagenesis. 2. Alteration of Asp172 to Glu (charged) or to Gln or Asn (polar but uncharged) produced functional channels showing inward rectification, though rectification was weaker with Gln and Asn. 3. Intrinsic gating around the potassium equilibrium potential, EK, was conserved only if the charge on residue 172 was conserved. Currents through channels with Gln or Asn in this position showed no time dependence under hyperpolarization. 4. The change from Asp to Gln also reduced the affinity for internal Mg2+ at least fivefold, indicating that Asp172 also forms part of the site for Mg2+ blockage. 5. The consequences for channel structure of Asp172 lining the pore are discussed.

我们通过定点诱变描述了改变小鼠内向整流钾通道IRK1跨膜α螺旋中天冬氨酸残基（Asp172）对通道功能的影响。2. 将Asp172替换为Glu（带电荷）、Gln或Asn（极性但不带电荷）产生了具有内向整流特性的功能性通道，不过Gln和Asn的整流作用较弱。3. 只有当172位残基的电荷保持不变时，围绕钾平衡电位EK的内在门控才得以保留。在超极化情况下，该位置为Gln或Asn的通道的电流没有时间依赖性。4. 从Asp变为Gln也使对内部Mg2+的亲和力至少降低了五倍，表明Asp172也是Mg2+阻断位点的一部分。5. 讨论了位于孔道内的Asp172对通道结构的影响。