BMRB: 4477

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, 3434.770 Da Detail

MISSVCVSSY RGRKXGNKPP XKTCLKEEMA

Formula weight

3434.77 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.3 %, Completeness: 97.7 %, Completeness (bb): 98.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	97.7 % (169 of 173)	97.7 % (169 of 173)
Backbone	98.2 % (55 of 56)	98.2 % (55 of 56)
Sidechain	97.4 % (114 of 117)	97.4 % (114 of 117)
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

MISSVCVSSY RGRKXGNKPP XKTCLKEEMA

Show sample condition

Sample

Temperature 283 K, pH 3.37

#	Name	Isotope labeling	Type	Concentration
1	Potassium channel

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Protein Blocks Logo

Calculated from 23 models in PDB: 1B4I, Strand ID: A Detail

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Release date

2002-06-06

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