2b3r
From Proteopedia
(New page: 200px<br /><applet load="2b3r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b3r, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:2b3r.gif|left|200px]]<br /><applet load="2b3r" size=" | + | [[Image:2b3r.gif|left|200px]]<br /><applet load="2b3r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b3r, resolution 2.3Å" /> | caption="2b3r, resolution 2.3Å" /> | ||
'''Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2'''<br /> | '''Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphatidylinositide (PtdIns) 3-kinase catalyzes the addition of a | + | 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 Structure== | ==About this Structure== | ||
| - | 2B3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 2B3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bellamy, H.]] | [[Category: Bellamy, H.]] | ||
| - | [[Category: Czech, M | + | [[Category: Czech, M P.]] |
[[Category: He, D.]] | [[Category: He, D.]] | ||
[[Category: Kita, A.]] | [[Category: Kita, A.]] | ||
| Line 22: | Line 22: | ||
[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Song, X.]] | [[Category: Song, X.]] | ||
| - | [[Category: Verbasius, J | + | [[Category: Verbasius, J V.]] |
| - | [[Category: Zhou, G | + | [[Category: Zhou, G W.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: c2 domain]] | [[Category: c2 domain]] | ||
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[[Category: pi3-kinase]] | [[Category: pi3-kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:50 2008'' |
Revision as of 14:33, 21 February 2008
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Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2
Overview
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 Structure
2B3R is a Single protein structure of sequence from Mus musculus with as ligand. Active as Phosphatidylinositol-4-phosphate 3-kinase, with EC number 2.7.1.154 Full crystallographic information is available from OCA.
Reference
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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