1zto: Difference between revisions
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|PDB= 1zto |SIZE=350|CAPTION= <scene name='initialview01'>1zto</scene> | |PDB= 1zto |SIZE=350|CAPTION= <scene name='initialview01'>1zto</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=AAR:ARGININEAMIDE'>AAR</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zto OCA], [http://www.ebi.ac.uk/pdbsum/1zto PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zto RCSB]</span> | |||
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[[Category: potassium channel]] | [[Category: potassium channel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:30 2008'' | ||
Revision as of 01:41, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES
OverviewOverview
The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.
About this StructureAbout this Structure
1ZTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of inactivation gates from mammalian voltage-dependent potassium channels., Antz C, Geyer M, Fakler B, Schott MK, Guy HR, Frank R, Ruppersberg JP, Kalbitzer HR, Nature. 1997 Jan 16;385(6613):272-5. PMID:9000078
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