2RED

Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.

Summary for 2RED

• Entry DOI: 10.2210/pdb2red/pdb
• Related: 2ar5 2rea
• Descriptor: Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide, GLYCEROL (3 entities in total)
• Functional Keywords: px domain, pi3k, kinase, transferase, nuclear protein, phosphoinositide, cytoplasmic vesicle, golgi apparatus, membrane, nucleus, phosphorylation
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane: O00443
• Total number of polymer chains: 1
• Total formula weight: 14928.13

Authors

Parkinson, G.N.,Vines, D.,Driscoll, P.C.,Djordjevic, S. (deposition date: 2007-09-26, release date: 2007-11-27, Last modification date: 2023-08-30)

Primary citation

Parkinson, G.N.,Vines, D.,Driscoll, P.C.,Djordjevic, S.
Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding
Bmc Struct.Biol., 8:13-13, 2008

PubMed Abstract: 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.

PubMed: 18312637
DOI: 10.1186/1472-6807-8-13

Experimental method

X-RAY DIFFRACTION (2.1 Å)