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-Structure paper
Title | A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 112, Page E3619-E3628, Year 2015 |
Publish date | Aug 20, 2014 (structure data deposition date) |
Authors | Napolitano, L.M. / Bisha, I. / De March, M. / Marchesi, A. / Arcangeletti, M. / Demitri, N. / Mazzolini, M. / Rodriguez, A. / Magistrato, A. / Onesti, S. ...Napolitano, L.M. / Bisha, I. / De March, M. / Marchesi, A. / Arcangeletti, M. / Demitri, N. / Mazzolini, M. / Rodriguez, A. / Magistrato, A. / Onesti, S. / Laio, A. / Torre, V. |
External links | Proc. Natl. Acad. Sci. USA / PubMed:26100907 |
Methods | X-ray diffraction |
Resolution | 2.3 - 2.85 Å |
Structure data | PDB-4r50: PDB-4r6z: PDB-4r7c: PDB-4r8c: PDB-4rai: PDB-4ro2: |
Chemicals | ChemComp-MPD: ChemComp-GLY: ChemComp-HOH: ChemComp-CS: ChemComp-DMN: ChemComp-RB: ChemComp-NA: ChemComp-3P8: |
Source |
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Keywords | TRANSPORT PROTEIN / Alpha helical membrane protein / chimera channel / ALPHA-HELICAL membrane protein / NaK-chimera channel in complex with DiMA+ / ion channel |