2red: Difference between revisions
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[[Image:2red.gif|left|200px]] | [[Image:2red.gif|left|200px]] | ||
'''Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.''' | {{Structure | ||
|PDB= 2red |SIZE=350|CAPTION= <scene name='initialview01'>2red</scene>, resolution 2.10Å | |||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Residue+A+302'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+A+303'>AC3</scene>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Residue+A+304'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+A+305'>AC5</scene> and <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+A+306'>AC6</scene> | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|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== | ||
2RED is a [ | 2RED 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=2RED 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 20: | Line 35: | ||
[[Category: nuclear protein]] | [[Category: nuclear protein]] | ||
[[Category: nucleus]] | [[Category: nucleus]] | ||
[[Category: phosphoinositide ]] | [[Category: phosphoinositide]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
[[Category: pi3k]] | [[Category: pi3k]] | ||
| Line 27: | Line 42: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
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