Dynamic conformational changes of extracellular S5–P linkers in the hERG channel

• Published in: The Journal of physiology Vol. 569; no. 1; pp. 75 - 89
• Main Authors: Jiang, Min, Zhang, Mei, Maslennikov, Innokenty V., Liu, Jie, Wu, Dong‐Mei, Korolkova, Yuliya V., Arseniev, Alexander S., Grishin, Eugene V., Tseng, Gea‐Ny
• Format: Journal Article
• Language: English
• Published: 9600 Garsington Road , Oxford , OX4 2DQ , UK Blackwell Science Ltd 15.11.2005; Blackwell Science Inc
• Subjects: Amino Acid Sequence; Binding Sites; Computer Simulation; Ether-A-Go-Go Potassium Channels - analysis; Ether-A-Go-Go Potassium Channels - chemistry; Extracellular Space - chemistry; Models, Chemical; Models, Molecular; Molecular and Genomic Physiology; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Subunits; Structure-Activity Relationship

The hERG channel has an unusually long ‘S5–P linker’ (residues 571–613) that lines the outer mouth of the pore. Previously, we have shown that residues along this S5–P linker are critical for the fast‐inactivation process and K+ selectivity of the hERG channel. Here we used several approaches to pro...