Structural basis for high-affinity phosphoinositide binding by pleckstrin homology domains.
نویسنده
چکیده
Regulation in Metabolism Group/Membrane Group Colloquium Organized by S. Cockcroft (Department of Physiology, University College London) and P. Hawkins (Department of Signalling, The Babraham Institute), Edited by S. Cockcroft and Sponsored by Eschelon Research Laboratory, Eli Lilly and Co., The Gatsby Charitable Foundation, Merck Sharpe and Dohme, Novartis, Smithkline Beecham, Unilever, Yamanouchi Research Institute and Zeneca. 668th Meeting held at the University of Glasgow, 7-9 April 1999.
منابع مشابه
Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains.
The pleckstrin homology (PH) domains of the homologous proteins Grp1 (general receptor for phosphoinositides), ARNO (Arf nucleotide binding site opener), and Cytohesin-1 bind phosphatidylinositol (PtdIns) 3,4,5-trisphosphate with unusually high selectivity. Remarkably, splice variants that differ only by the insertion of a single glycine residue in the beta1/beta2 loop exhibit dual specificity ...
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Phosphoinositides (PIs) are a class of phospholipids that are involved in cellular signaling, organelle identity and membrane trafficking. We have applied structural bioinformatics techniques in an attempt to predict the affinity and specificity of protein structures for phosphoinositide compounds. The ability to predict whether a protein is able to recognize phosphoinositide compounds would fo...
متن کاملMolecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides.
More than 250 pleckstrin homology (PH) domains have been identified in the human proteome. All PH domains studied to date appear to bind phosphoinositides, most binding only weakly and non-specifically. Members of a small subclass of PH domains show both high affinity and specificity for particular phosphoinositides, and recent structural studies have provided detailed views of these specific i...
متن کاملPleckstrin homology (PH) domains and phosphoinositides.
PH (pleckstrin homology) domains represent the 11th most common domain in the human proteome. They are best known for their ability to bind phosphoinositides with high affinity and specificity, although it is now clear that less than 10% of all PH domains share this property. Cases in which PH domains bind specific phosphoinositides with high affinity are restricted to those phosphoinositides t...
متن کاملStructural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.
Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal-dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two ...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 27 4 شماره
صفحات -
تاریخ انتشار 1999