Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6613
|
| pubmed:dateCreated |
1997-2-6
|
| pubmed:databankReference | |
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0028-0836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
385
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
272-5
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9000078-Amino Acid Sequence,
pubmed-meshheading:9000078-Animals,
pubmed-meshheading:9000078-Electrochemistry,
pubmed-meshheading:9000078-Ion Channel Gating,
pubmed-meshheading:9000078-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9000078-Mammals,
pubmed-meshheading:9000078-Models, Molecular,
pubmed-meshheading:9000078-Molecular Sequence Data,
pubmed-meshheading:9000078-Peptide Fragments,
pubmed-meshheading:9000078-Potassium Channels,
pubmed-meshheading:9000078-Protein Conformation,
pubmed-meshheading:9000078-Structure-Activity Relationship
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
NMR structure of inactivation gates from mammalian voltage-dependent potassium channels.
|
| pubmed:affiliation |
Institute of Physiology, University of Tubingen, Germany.
|
| pubmed:publicationType |
Journal Article
|