1QG9
SECOND REPEAT (IS2MIC) FROM VOLTAGE-GATED SODIUM CHANNEL
Summary for 1QG9
| Entry DOI | 10.2210/pdb1qg9/pdb |
| Descriptor | PROTEIN (SODIUM CHANNEL PROTEIN, BRAIN II ALPHA SUBUNIT) (1 entity in total) |
| Functional Keywords | transmembrane sodium channel, transmembrane channel |
| Cellular location | Membrane; Multi-pass membrane protein: P08104 |
| Total number of polymer chains | 1 |
| Total formula weight | 2480.85 |
| Authors | Doak, D.J.,Mulvey, D.,Kawaguchi, K.,Villalain, J.,Campbell, I.D. (deposition date: 1999-04-22, release date: 1999-04-30, Last modification date: 2023-12-27) |
| Primary citation | Doak, D.G.,Mulvey, D.,Kawaguchi, K.,Villalain, J.,Campbell, I.D. Structural studies of synthetic peptides dissected from the voltage-gated sodium channel. J.Mol.Biol., 258:672-687, 1996 Cited by PubMed Abstract: Peptides representing transmembrane regions of the alpha-subunit of the voltage-gated sodium channel were synthesised and their structures analysed, using 1H NMR and CD, in trifluoroethanol and in dodecylphosphocholine micelles. Sequence analysis suggests that the channel has six regions, S1 to S6, predicted to span the membrane in four homologous domains, designated, I, II, III and IV. Presented here are studies of representatives examples of possible single spanning segments (IS2, IS4, IVS4) and a double spanning segment, IS34, composed of segments IS3 and IS4. In addition, we investigated ISlink56, the putative linker region between segments IS5 and IS6. All of the peptides were found to have predominantly alpha-helical structures in both solvent systems. There was some evidence for bending of the longer helices but there was no discernible evidence for well-defined tertiary structure. PubMed: 8637001DOI: 10.1006/jmbi.1996.0278 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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