2b3r: Difference between revisions
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|PDB= 2b3r |SIZE=350|CAPTION= <scene name='initialview01'>2b3r</scene>, resolution 2.3Å | |PDB= 2b3r |SIZE=350|CAPTION= <scene name='initialview01'>2b3r</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | |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, Cpk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Pik3c2a, Cpk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3r OCA], [http://www.ebi.ac.uk/pdbsum/2b3r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b3r RCSB]</span> | |||
}} | }} | ||
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[[Category: Verbasius, J V.]] | [[Category: Verbasius, J V.]] | ||
[[Category: Zhou, G W.]] | [[Category: Zhou, G W.]] | ||
[[Category: c2 domain]] | [[Category: c2 domain]] | ||
[[Category: lipid binding]] | [[Category: lipid binding]] | ||
[[Category: pi3-kinase]] | [[Category: pi3-kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:01 2008'' |
Revision as of 02:01, 31 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | |||||||
Gene: | Pik3c2a, Cpk (Mus musculus) | ||||||
Activity: | Phosphatidylinositol-4-phosphate 3-kinase, with EC number 2.7.1.154 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2
OverviewOverview
Phosphatidylinositide (PtdIns) 3-kinase catalyzes the addition of a phosphate group to the 3'-position of phosphatidyl inositol. Accumulated evidence shows that PtdIns 3-kinase can provide a critical signal for cell proliferation, cell survival, membrane trafficking, glucose transport, and membrane ruffling. Mammalian PtdIns 3-kinases are divided into three classes based on structure and substrate specificity. A unique characteristic of class II PtdIns 3-kinases is the presence of both a phox homolog domain and a C2 domain at the C terminus. The biological function of the C2 domain of the class II PtdIns 3-kinases remains to be determined. We have determined the crystal structure of the mCPK-C2 domain, which is the first three-dimensional structural model of a C2 domain of class II PtdIns 3-kinases. Structural studies reveal that the mCPK-C2 domain has a typical anti-parallel beta-sandwich fold. Scrutiny of the surface of this C2 domain has identified three small, shallow sulfate-binding sites. On the basis of the structural features of these sulfate-binding sites, we have studied the lipid binding properties of the mCPK-C2 domain by site-directed mutagenesis. Our results show that this C2 domain binds specifically to PtdIns(3,4)P(2) and PtdIns(4,5)P(2) and that three lysine residues at SBS I site, Lys-1420, Lys-1432, and Lys-1434, are responsible for the phospholipid binding affinity.
About this StructureAbout this Structure
2B3R is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha., Liu L, Song X, He D, Komma C, Kita A, Virbasius JV, Huang G, Bellamy HD, Miki K, Czech MP, Zhou GW, J Biol Chem. 2006 Feb 17;281(7):4254-60. Epub 2005 Dec 7. PMID:16338929
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