3SUA

Crystal structure of the intracellular domain of Plexin-B1 in complex with Rac1

3SUA の概要

• エントリーDOI: 10.2210/pdb3sua/pdb
• 関連するPDBエントリー: 3SU8
• 分子名称: Ras-related C3 botulinum toxin substrate 1, Plexin-B1, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: axon guidance, signal transduction, apoptosis-signaling protein complex, apoptosis/signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted: P63000; Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): O43157
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 281530.03

構造登録者

Bell, C.H.,Aricescu, A.R.,Jones, E.Y.,Siebold, C. (登録日: 2011-07-11, 公開日: 2011-09-07, 最終更新日: 2024-02-28)

主引用文献

Bell, C.H.,Aricescu, A.R.,Jones, E.Y.,Siebold, C.
A Dual Binding Mode for RhoGTPases in Plexin Signalling.
Plos Biol., 9:e1001134-e1001134, 2011

PubMed Abstract: Plexins are cell surface receptors for the semaphorin family of cell guidance cues. The cytoplasmic region comprises a Ras GTPase-activating protein (GAP) domain and a RhoGTPase binding domain. Concomitant binding of extracellular semaphorin and intracellular RhoGTPase triggers GAP activity and signal transduction. The mechanism of this intricate regulation remains elusive. We present two crystal structures of the human Plexin-B1 cytoplasmic region in complex with a constitutively active RhoGTPase, Rac1. The structure of truncated Plexin-B1-Rac1 complex provides no mechanism for coupling RhoGTPase and Ras binding sites. On inclusion of the juxtamembrane helix, a trimeric structure of Plexin-B1-Rac1 complexes is stabilised by a second, novel, RhoGTPase binding site adjacent to the Ras site. Site-directed mutagenesis combined with cellular and biophysical assays demonstrate that this new binding site is essential for signalling. Our findings are consistent with a model in which extracellular and intracellular plexin clustering events combine into a single signalling output.

PubMed: 21912513
DOI: 10.1371/journal.pbio.1001134

実験手法

X-RAY DIFFRACTION (4.39 Å)