2rea

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
|SITE=
|SITE=
|LIGAND=
|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]
+
|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>
|GENE= PIK3C2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= PIK3C2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2ar5|2ar5]], [[2red|2RED]]
 +
|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>
}}
}}
Line 41: Line 44:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:35:14 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:59:27 2008''

Revision as of 01:59, 31 March 2008

Image:2rea.gif


PDB ID 2rea

Drag the structure with the mouse to rotate
, resolution 2.50Å
Gene: PIK3C2A (Homo sapiens)
Activity: Phosphatidylinositol-4-phosphate 3-kinase, with EC number 2.7.1.154
Related: 2ar5, 2RED


Resources: FirstGlance, OCA, PDBsum, RCSB
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 Mon Mar 31 04:59:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rea"
Personal tools