[Structural basis of the K+ channel inhibition by pore-blocking toxins, revealed by NMR].
Takeuchi
Koh
K
shimada@iw.nmr.f.u-tokyo.ac.jp
Shimada
Ichio
I
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry* / Q000378:metabolism; D026902:Potassium Channel Blockers / Q000737:chemistry* / Q000378:metabolism; D015221:Potassium Channels / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012604:Scorpion Venoms / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D008024:Ligands; D008565:Membrane Proteins; D009498:Neurotoxins; D026902:Potassium Channel Blockers; D015221:Potassium Channels; D012604:Scorpion Venoms; C107790:prokaryotic potassium channel; C087603:agitoxin 2