4A6H
Crystal structure of Slm1-PH domain in complex with Inositol-4- phosphate
Summary for 4A6H
| Entry DOI | 10.2210/pdb4a6h/pdb |
| Related | 4A6F 4A6K |
| Descriptor | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE-BINDING PROTEIN SLM1, PHOSPHATE ION, D-MYO-INOSITOL-4-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | signaling protein |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P40485 |
| Total number of polymer chains | 4 |
| Total formula weight | 56650.64 |
| Authors | Anand, K.,Maeda, K.,Gavin, A.C. (deposition date: 2011-11-03, release date: 2012-06-13, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 22574179DOI: 10.1371/JOURNAL.PONE.0036526 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.449 Å) |
Structure validation
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