2rea

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[[Image:2rea.gif|left|200px]]
[[Image:2rea.gif|left|200px]]
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{{Structure
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|PDB= 2rea |SIZE=350|CAPTION= <scene name='initialview01'>2rea</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2rea", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= PIK3C2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2rea| PDB=2rea | SCENE= }}
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|RELATEDENTRY=[[2ar5|2ar5]], [[2red|2RED]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rea OCA], [http://www.ebi.ac.uk/pdbsum/2rea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rea RCSB]</span>
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'''Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.'''
'''Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.'''
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[[Category: Parkinson, G N.]]
[[Category: Parkinson, G N.]]
[[Category: Vines, D.]]
[[Category: Vines, D.]]
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[[Category: cytoplasm]]
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[[Category: Cytoplasm]]
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[[Category: cytoplasmic vesicle]]
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[[Category: Cytoplasmic vesicle]]
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[[Category: golgi apparatus]]
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[[Category: Golgi apparatus]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: nuclear protein]]
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[[Category: Nuclear protein]]
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[[Category: nucleus]]
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[[Category: Nucleus]]
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[[Category: phosphoinositide]]
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[[Category: Phosphoinositide]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: pi3k]]
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[[Category: Pi3k]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: px domain]]
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[[Category: Px domain]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:44:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:59:27 2008''
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Revision as of 13:44, 4 May 2008

Image:2rea.gif

Template:STRUCTURE 2rea

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 Sun May 4 16:44:08 2008

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