Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents



ID: 22539.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
Structure of the inactivating gate from the Shaker voltage gated K+ channel analyzed by NMR spectroscopy
Translation of Title:Structure of the inactivating gate from the Shaker voltage gated K<SUP>+</SUP> channel analyzed by NMR spectroscopy
Authors:Schott, M. K.; Antz, C.; Frank, R.; Ruppersberg, J. Peter; Kalbitzer, Hans Robert
Language:English
Date of Publication (YYYY-MM-DD):1998
Title of Journal:Eur. Biophys. J.
Journal Abbrev.:Eur. Biophys. J.
Volume:27
Start Page:99
End Page:104
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Rapid inactivation of voltage-gated K+ (Kv) channels is mediated by an N-terminal domain (inactivating ball domain) which blocks the open channel from the cytoplasmic side. Inactivating ball domains of various Kv channels are also biologically active when synthesized separately and added as a peptide to the solution. Synthetic inactivating ball domains from different Kv channels with hardly any sequence homology mediate quite similar effects even on unrelated Kv channel subtypes whose inactivation domain has been deleted. The solution structure of the inactivating ball peptide from Shaker (Sh-P22) was analyzed with NMR spectroscopy. The NMR data indicate a non-random structure in an aqueous environment. However, while other inactivating ball peptides showed well-defined three-dimensional structures under these conditions, Sh-P22 does not have a unique, compactly folded structure in solution.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Zellphysiologie/
Identifiers:URI:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [Abstract]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.