Title |
Structural Analyses of the Slm1-PH Domain Demonstrate Ligand Binding in the Non-Canonical Site
|
---|---|
Published in |
PLOS ONE, May 2012
|
DOI | 10.1371/journal.pone.0036526 |
Pubmed ID | |
Authors |
Kanchan Anand, Kenji Maeda, Anne-Claude Gavin |
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. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 35 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 12 | 34% |
Student > Master | 7 | 20% |
Researcher | 4 | 11% |
Student > Bachelor | 3 | 9% |
Professor | 2 | 6% |
Other | 3 | 9% |
Unknown | 4 | 11% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 17 | 49% |
Biochemistry, Genetics and Molecular Biology | 8 | 23% |
Chemistry | 3 | 9% |
Unspecified | 1 | 3% |
Veterinary Science and Veterinary Medicine | 1 | 3% |
Other | 2 | 6% |
Unknown | 3 | 9% |