Stocker M, Miller C
Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
Proc Natl Acad Sci U S A. 1994 Sep 27;91(20):9509-13. doi: 10.1073/pnas.91.20.9509.
Many voltage-gated K+ channels carry in the external vestibule a receptor for charybdotoxin, a peptide channel blocker. We use point mutagenesis of both charybdotoxin and a Shaker K+ channel to isolate the electrostatic interaction energy between chosen pairs of residues, one on the channel and one on bound toxin. The results allow estimates of physical distances between such residue pairs and, in combination with the known structure of charybdotoxin, localize specific channel residues in three-dimensional space.
许多电压门控钾离子通道在外部前庭携带一种肽通道阻滞剂——芋螺毒素的受体。我们对芋螺毒素和一种Shaker钾离子通道进行点突变,以分离所选残基对之间的静电相互作用能,其中一个残基在通道上,另一个在结合的毒素上。这些结果有助于估计此类残基对之间的物理距离,并结合芋螺毒素的已知结构,在三维空间中定位特定的通道残基。