+検索条件
-Structure paper
タイトル | Structural insight into TRPV5 channel function and modulation. |
---|---|
ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 116, Issue 18, Page 8869-8878, Year 2019 |
掲載日 | 2019年4月30日 |
著者 | Shangyu Dang / Mark K van Goor / Daniel Asarnow / YongQiang Wang / David Julius / Yifan Cheng / Jenny van der Wijst / |
PubMed 要旨 | TRPV5 (transient receptor potential vanilloid 5) is a unique calcium-selective TRP channel essential for calcium homeostasis. Unlike other TRPV channels, TRPV5 and its close homolog, TRPV6, do not ...TRPV5 (transient receptor potential vanilloid 5) is a unique calcium-selective TRP channel essential for calcium homeostasis. Unlike other TRPV channels, TRPV5 and its close homolog, TRPV6, do not exhibit thermosensitivity or ligand-dependent activation but are constitutively open at physiological membrane potentials and modulated by calmodulin (CaM) in a calcium-dependent manner. Here we report high-resolution electron cryomicroscopy structures of truncated and full-length TRPV5 in lipid nanodiscs, as well as of a TRPV5 W583A mutant and TRPV5 in complex with CaM. These structures highlight the mechanism of calcium regulation and reveal a flexible stoichiometry of CaM binding to TRPV5. |
リンク | Proc Natl Acad Sci U S A / PubMed:30975749 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.8 - 3.3 Å |
構造データ | |
化合物 | ChemComp-CA: |
由来 |
|
キーワード | MEMBRANE PROTEIN / ion channel / TRP channel |