2L4R
NMR solution structure of the N-terminal PAS domain of hERG
Summary for 2L4R
| Entry DOI | 10.2210/pdb2l4r/pdb |
| Descriptor | Potassium voltage-gated channel subfamily H member 2 (1 entity in total) |
| Functional Keywords | herg, potassium channel, pas domain, eag domain, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein: Q12809 |
| Total number of polymer chains | 1 |
| Total formula weight | 15298.81 |
| Authors | |
| Primary citation | Li, Q.,Gayen, S.,Chen, A.S.,Huang, Q.,Raida, M.,Kang, C. NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker. Biochem.Biophys.Res.Commun., 403:126-132, 2010 Cited by PubMed Abstract: The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or mis-translocation. To study the structure of NTD, it was overexpressed and purified from Escherichia coli cells using affinity purification and gel filtration chromatography. The purified protein behaved as a monomer under purification conditions. Far- and near-UV, circular dichroism (CD) and solution nuclear magnetic resonance (NMR) studies showed that the purified protein was well-folded. The solution structure of NTD was obtained and the N-terminal residues 13-23 forming an amphipathic helix which may be important for the protein-protein or protein-membrane interactions. NMR titration experiment also demonstrated that residues from 88 to 94 in NTD are important for the molecular interaction with the peptide derived from the S4-S5 linker. PubMed: 21055387DOI: 10.1016/j.bbrc.2010.10.132 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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