| Literature DB >> 19427861 |
Yu-hang Chen1, Lin-ling He, Douglas R Buchanan, Yun Zhang, Aileen Fitzmaurice, Jian Yang.
Abstract
The beta-subunit of voltage-gated Ca(2+) channels is essential for trafficking the channels to the plasma membrane and regulating their gating. It contains a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain, which interact intramolecularly. We investigated the structural underpinnings of this intramolecular coupling and found that in addition to a previously described SH3 domain beta strand, two structural elements are crucial for maintaining a strong and yet potentially modifiable SH3-GK intramolecular coupling: an intrinsically weak SH3-GK interface and a direct connection of the SH3 and GK domains. Alterations of these elements uncouple the two functions of the beta-subunit, degrading its ability to regulate gating while leaving its chaperone effect intact.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19427861 PMCID: PMC2739582 DOI: 10.1016/j.febslet.2009.05.001
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124