4A6F

Crystal structure of Slm1-PH domain in complex with Phosphoserine

4A6F の概要

• エントリーDOI: 10.2210/pdb4a6f/pdb
• 関連するPDBエントリー: 4A5K 4A6H 4A6K
• 分子名称: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE-BINDING PROTEIN SLM1, PHOSPHATE ION, PHOSPHOSERINE, ... (5 entities in total)
• 機能のキーワード: signaling protein, post translational modification
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28462.43

構造登録者

Anand, K.,Maeda, K.,Gavin, A.C. (登録日: 2011-11-02, 公開日: 2012-06-13, 最終更新日: 2023-12-20)

主引用文献

Anand, K.,Maeda, K.,Gavin, A.C.
Structural Analyses of Slm1-Ph Domain Demonstrate Ligand Binding in the Non-Canonical Site
Plos One, 7:36526-, 2012

PubMed Abstract: Pleckstrin homology (PH) domains are common membrane-targeting modules and their best characterized ligands are a set of important signaling lipids that include phosphatidylinositol phosphates (PtdInsPs). PH domains recognize PtdInsPs through two distinct mechanisms that use different binding pockets on opposite sides of the β-strands 1 and 2: i) a canonical binding site delimited by the β1-β2 and β3-β4loops and ii) a non-canonical binding site bordered by the β1-β2 and β5-β6loops. The PH domain-containing protein Slm1 from budding yeast Saccharomyces cerevisiae is required for actin cytoskeleton polarization and cell growth. We recently reported that this PH domain binds PtdInsPs and phosphorylated sphingolipids in a cooperative manner.

PubMed: 22574179
DOI: 10.1371/JOURNAL.PONE.0036526

実験手法

X-RAY DIFFRACTION (1.68 Å)