[NMR study on solution configuration of mHCN1 pore peptide].
Spin systems for amino acid residues in mHCN1 pore region peptide have been identified through analysis of 2D NMR spectra. The sequence-specific assignment of spin systems was obtained by NOEs correlation in WET-NOESY spectra, and the complete assignment of proton resonances for backbone and side chain has been achieved. CNS software was used to calculate the structure of mHCN1 19 aa peptide. The results show that an alpha-helix from residue 10 to residue 13 is formed within the pore region. The results of NMR study on mHCN1 pore peptide provide the basis for further understanding the mechanism of ion selectivity of channels.
Sui
Tao
T
Institute of Materia Medica, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.
Yu
Han-Gang
HG
Hu
Hong-Yu
HY
Shi
Yan-Hong
YH
Song
Guo-Qiang
GQ
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D054815:Cyclic Nucleotide-Gated Cation Channels; D064428:Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; D007473:Ion Channels / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D015221:Potassium Channels
D054815:Cyclic Nucleotide-Gated Cation Channels; D064428:Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; D007473:Ion Channels; D015221:Potassium Channels