BMRB: 4476

Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate

Authors

Antz, C., Bauer, T., Kalbacher, H., Frank, R., Covarrubias, M., Kalbitzer, H.R., Ruppersberg, J.P., Baukrowitz, T., Fakler, B.

Assembly

Potassium channel

Entity

1. Potassium channel (polymer, Thiol state: not reported), 30 monomers, 3354.791 Da Detail

MISSVCVXSY RGRKSGNKPP SKTCLKEEMA

Formula weight

3354.791 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.7 %, Completeness: 97.7 %, Completeness (bb): 98.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	97.7 % (173 of 177)	97.7 % (173 of 177)
Backbone	98.3 % (57 of 58)	98.3 % (57 of 58)
Sidechain	97.5 % (116 of 119)	97.5 % (116 of 119)
Aromatic	100.0 % (4 of 4)	100.0 % (4 of 4)
Methyl	100.0 % (10 of 10)	100.0 % (10 of 10)

1. Potassium channel

MISSVCVXSY RGRKSGNKPP SKTCLKEEMA

Show sample condition

Sample

Temperature 283 K, pH 3.51

#	Name	Isotope labeling	Type	Concentration
1	Potassium channel			0.0 ~ 0.0 mM

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Protein Blocks Logo

Calculated from 22 models in PDB: 1B4G, Strand ID: A Detail

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Release date

2002-06-10

Citation

NMR structure of inactivation gates from mammalian voltage-dependent potassium channels
Antz, C., Geyer, M., Fakler, B., Schott, M.K., Guy, H.R., Frank, R., Ruppersberg, J.P., Kalbitzer, H.R.
Nature (1997), 385, 272-275, PubMed 9000078 , DOI 10.1038/385272a0 , Abstract

Related entities 1. Potassium channel, : 1 : 8 : 3 entities Detail

Interaction partners 1. Potassium channel, : 1 interactors Detail

Experiments performed 1 experiments Detail