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2rea
From Proteopedia
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| - | [[Image:2rea.gif|left|200px]] | + | [[Image:2rea.gif|left|200px]] |
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| - | '''Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.''' | + | {{Structure |
| + | |PDB= 2rea |SIZE=350|CAPTION= <scene name='initialview01'>2rea</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphatidylinositol-4-phosphate_3-kinase Phosphatidylinositol-4-phosphate 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.154 2.7.1.154] | ||
| + | |GENE= PIK3C2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.''' | ||
| + | |||
| + | |||
| + | ==Overview== | ||
| + | ABSTRACT: BACKGROUND: PX domains have specialized protein structures involved in binding of phosphoinositides (PIs). Through binding to the various PIs PX domains provide site-specific membrane signals to modulate the intracellular localisation and biological activity of effector proteins. Several crystal structures of these domains are now available from a variety of proteins. All PX domains contain a canonical core structure with main differences exhibited within the loop regions forming the phosphoinositide binding pockets. It is within these areas that the molecular basis for ligand specificity originates. RESULTS: We now report two new structures of PI3K-C2 PX domain that crystallised in a P3121 space group. The two structures, refined to 2.1 A and 2.5 A, exhibit significantly different conformations of the phosphoinositide-binding loops. Unexpectedly, in one of the structures, we have detected a putative-ligand trapped in the binding site during the process of protein purification and crystallisation. CONCLUSIONS: The two structures reported here provide a more complete description of the phosphoinositide binding region compared to the previously reported 2.6 A crystal structure of human PI3K-C2 PX where this region was highly disordered. The structures enabled us to further analyse PI specificity and to postulate that the observed conformational change could be related to ligand-binding. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2REA is a [ | + | 2REA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REA OCA]. |
| + | |||
| + | ==Reference== | ||
| + | Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding., Parkinson GN, Vines D, Driscoll PC, Djordjevic S, BMC Struct Biol. 2008 Feb 29;8(1):13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18312637 18312637] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphatidylinositol-4-phosphate 3-kinase]] | [[Category: Phosphatidylinositol-4-phosphate 3-kinase]] | ||
| Line 26: | Line 41: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:35:14 2008'' |
Revision as of 16:35, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PIK3C2A (Homo sapiens) | ||||||
| Activity: | Phosphatidylinositol-4-phosphate 3-kinase, with EC number 2.7.1.154 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.
Overview
ABSTRACT: BACKGROUND: PX domains have specialized protein structures involved in binding of phosphoinositides (PIs). Through binding to the various PIs PX domains provide site-specific membrane signals to modulate the intracellular localisation and biological activity of effector proteins. Several crystal structures of these domains are now available from a variety of proteins. All PX domains contain a canonical core structure with main differences exhibited within the loop regions forming the phosphoinositide binding pockets. It is within these areas that the molecular basis for ligand specificity originates. RESULTS: We now report two new structures of PI3K-C2 PX domain that crystallised in a P3121 space group. The two structures, refined to 2.1 A and 2.5 A, exhibit significantly different conformations of the phosphoinositide-binding loops. Unexpectedly, in one of the structures, we have detected a putative-ligand trapped in the binding site during the process of protein purification and crystallisation. CONCLUSIONS: The two structures reported here provide a more complete description of the phosphoinositide binding region compared to the previously reported 2.6 A crystal structure of human PI3K-C2 PX where this region was highly disordered. The structures enabled us to further analyse PI specificity and to postulate that the observed conformational change could be related to ligand-binding.
About this Structure
2REA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding., Parkinson GN, Vines D, Driscoll PC, Djordjevic S, BMC Struct Biol. 2008 Feb 29;8(1):13. PMID:18312637
Page seeded by OCA on Thu Mar 20 18:35:14 2008
Categories: Homo sapiens | Phosphatidylinositol-4-phosphate 3-kinase | Single protein | Djordjevic, S. | Driscoll, P C. | Parkinson, G N. | Vines, D. | Cytoplasm | Cytoplasmic vesicle | Golgi apparatus | Kinase | Membrane | Nuclear protein | Nucleus | Phosphoinositide | Phosphorylation | Pi3k | Polymorphism | Px domain | Transferase
