4A6H

Crystal structure of Slm1-PH domain in complex with Inositol-4- phosphate

4A6H の概要

• エントリーDOI: 10.2210/pdb4a6h/pdb
• 関連するPDBエントリー: 4A6F 4A6K
• 分子名称: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE-BINDING PROTEIN SLM1, PHOSPHATE ION, D-MYO-INOSITOL-4-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: signaling protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P40485
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56650.64

構造登録者

Anand, K.,Maeda, K.,Gavin, A.C. (登録日: 2011-11-03, 公開日: 2012-06-13, 最終更新日: 2024-05-01)

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 (1.449 Å)