Effects of Metal-Binding Properties of Human Kv Channel-Interacting Proteins on their Molecular Structure and Binding with Kv4.2 Channel View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-07

AUTHORS

Ching-Ping Chen, Liya Lee, Long-Sen Chang

ABSTRACT

The goal of the present study is to explore whether Ca2+ and Mg2+-binding properties of isomeric Kv channel-interacting proteins (KChIPs) have different effects on their molecular structure and the binding with Kv channel. 8-Anilinonaphthalene- 1-sulfonate fluorescence measurement showed that KChIP4.1 and KChIP2.2 possessed one and two types of Ca2+-binding sites, respectively, and only one type of Mg2+-binding site was noted in the two KChIP proteins. Removal of EF-hand 4 (EF-4) caused a marked drop in their high affinities for Ca2+, but the binding affinity for Mg2+ remained mostly the same. Unlike KChIP4.1, the intact EF-4 was essential for the Kv channel-binding ability of KChIP2.2 in a metal-free buffer. Nevertheless, the interaction of wild-type KChIPs and EF-4-truncated mutants with Kv channel was enhanced by the addition of Mg2+ and Ca2+. In contrast to KChIP4.1, the thermal stability of KChIP2.2 was decreased by the binding of Mg2+ and Ca2+. These results suggest that the conformational change with metal-bound KChIP4.1 is crucial for its interaction with Kv channel but not for KChIP2.2, and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and KChIP4.1 have different effects on their molecular structure. More... »

PAGES

345-351

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10930-006-9020-9

DOI

http://dx.doi.org/10.1007/s10930-006-9020-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011825891

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16951992


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