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Search query: phosphatidylinositol

90 articles match your search "phosphatidylinositol"

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Structures of the yeast Sec14-like phosphatidylinositol transfer protein Sfh2 in complex with phosphatidylinositol and squalene reveal structural determinants for ligand recognition.

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The crystal structure of phosphatidylinositol 4-kinase (PI4K) IIβ reveals new details such as the high conformational heterogeneity of the lateral hydrophobic pocket and, together with the structure of PI4K IIα with a nucleoside analogue, provides a structural basis for isoform-specific inhibitor design.

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The PH-GRAM domain of human MTMR4 was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 3.20 Å resolution.

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Human myotubularin-related protein 1 (MTMR1) was crystallized using polyethylene glycol 20 000 as a precipitant. Diffraction data have been collected to 2.0 Å resolution using synchrotron X-rays.

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The crystal structure of the PX (phox homology) domain of the Saccharomyces cerevisiae Vps17p protein was determined. The absence of basic residues around the canonical binding site suggests an inability to bind phosphatidylinositol phosphate molecules.

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Human myotubularin-related protein 3 was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 3.3 Å resolution.

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The crystal structure of human PI3K p85β iSH2 domain has been determined to 3.3 Å resolution. Comparison with the published structure of the bovine p85β iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. Structural analysis of human and bovine p85β iSH2 domains reveals conformational plasticity in the interhelical turn region of the coiled-coil motif.

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The crystal structure of human inositol monophosphatase in complex with the substrate-based inhibitor L-690,330 is reported.

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The structure of the putative membrane-binding tandem PX-PH domain module of the yeast protein Bem3 is reported.

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The structure of the Monkeypox virus protein A42R has been determined at a resolution of 1.52 Å. This protein has a backbone structure similar to that of cellular profilin, but structural variation in loop regions and a surface basic patch support biochemical data showing that this protein has distinct binding interactions with actin and phosphatidylinositol lipids and is not likely to bind proline-rich domain proteins or microtubules.
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