2b3r: Difference between revisions

Revision as of 02:13, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b3r.png

Template:STRUCTURE 2b3r

Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2

Template:ABSTRACT PUBMED 16338929

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16338929}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16338929 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16338929}}
 ==About this Structure==
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 [[Category: Lipid binding]]
 [[Category: Pi3-kinase]]
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