2MAH

Solution structure of Smoothened

2MAH の概要

• エントリーDOI: 10.2210/pdb2mah/pdb
• NMR情報: BMRB: 19354
• 分子名称: Protein smoothened (1 entity in total)
• 機能のキーワード: smoothened, hedgehog, oncoprotein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P91682
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14881.30

構造登録者

Rana, R.,Lee, H.,Zheng, J.J. (登録日: 2013-07-09, 公開日: 2014-03-05, 最終更新日: 2024-11-20)

主引用文献

Rana, R.,Carroll, C.E.,Lee, H.J.,Bao, J.,Marada, S.,Grace, C.R.,Guibao, C.D.,Ogden, S.K.,Zheng, J.J.
Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling.
Nat Commun, 4:2965-2965, 2013

PubMed Abstract: Smoothened (Smo) is a member of the Frizzled (FzD) class of G-protein-coupled receptors (GPCRs), and functions as the key transducer in the Hedgehog (Hh) signalling pathway. Smo has an extracellular cysteine-rich domain (CRD), indispensable for its function and downstream Hh signalling. Despite its essential role, the functional contribution of the CRD to Smo signalling has not been clearly elucidated. However, given that the FzD CRD binds to the endogenous Wnt ligand, it has been proposed that the Smo CRD may bind its own endogenous ligand. Here we present the NMR solution structure of the Drosophila Smo CRD, and describe interactions between the glucocorticoid budesonide (Bud) and the Smo CRDs from both Drosophila and human. Our results highlight a function of the Smo CRD, demonstrating its role in binding to small-molecule modulators.

PubMed: 24351982
DOI: 10.1038/ncomms3965

実験手法

SOLUTION NMR