The Structure of PI3K: Difference between revisions

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====Src Homology 2 (SH2) Domains====

<scene name='User:David_Canner/Sandbox_P/Sh2_open/1'>PI3K has two SH2 domains</scene>, an N-terminal (nSH2) domain and a C-terminal (CSH2) domain. <ref name="Flip"/> Both domains recognize similar consensus phosphorylated tyrosine motifs with the pattern: pY-V-X-M in activated receptors and adaptor proteins like PDGF, erbB3, c-Kit and CSF-1 receptors. <ref name="Weber">PMID:11123912</ref> It is upon the interaction of receptor and SH2 domain that the heterodimeric PI3K complex is activated. <ref name="Miled"> The <scene name='User:David_Canner/Sandbox_P/Sh2/2'>docking site for receptor in NSH2 is defined by the conserved residues Arg 340, Arg 358, and Thr 371</scene> ([[2iui]]), all of which coordinate the phosphorylated tyrosoine phosphate group.<ref name="Nolte"> PMID:8599763</ref> nSH2 was found to interact with the catalytic subunit directly, forming a broad-based scaffold for p110α and coordinates communication between the interacting domains. (Discussed Below). <ref name="Amzel"/>

<scene name='User:David_Canner/Sandbox_P/Sh2_open/1'>PI3K has two SH2 domains</scene>, an N-terminal (nSH2) domain and a C-terminal (CSH2) domain. <ref name="Flip"/> Both domains recognize similar consensus phosphorylated tyrosine motifs with the pattern: pY-V-X-M in activated receptors and adaptor proteins like PDGF, erbB3, c-Kit and CSF-1 receptors. <ref name="Weber">PMID:11123912</ref> It is upon the interaction of receptor and SH2 domain that the heterodimeric PI3K complex is activated. <ref name="Miled"/> The <scene name='User:David_Canner/Sandbox_P/Sh2/2'>docking site for receptor in NSH2 is defined by the conserved residues Arg 340, Arg 358, and Thr 371</scene> ([[2iui]]), all of which coordinate the phosphorylated tyrosoine phosphate group.<ref name="Nolte"> PMID:8599763</ref> nSH2 was found to interact with the catalytic subunit directly, forming a broad-based scaffold for p110α and coordinates communication between the interacting domains. (Discussed Below). <ref name="Amzel"/>

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The Structure of PI3K: Difference between revisions

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 ====Src Homology 2 (SH2) Domains====
-<scene name='User:David_Canner/Sandbox_P/Sh2_open/1'>PI3K has two SH2 domains</scene>, an N-terminal (nSH2) domain and a C-terminal (CSH2) domain. <ref name="Flip"/> Both domains recognize similar consensus phosphorylated tyrosine motifs with the pattern: pY-V-X-M in activated receptors and adaptor proteins like PDGF, erbB3, c-Kit and CSF-1 receptors. <ref name="Weber">PMID:11123912</ref> It is upon the interaction of receptor and SH2 domain that the heterodimeric PI3K complex is activated. <ref name="Miled"> The <scene name='User:David_Canner/Sandbox_P/Sh2/2'>docking site for receptor in NSH2 is defined by the conserved residues Arg 340, Arg 358, and Thr 371</scene> ([[2iui]]), all of which coordinate the phosphorylated tyrosoine phosphate group.<ref name="Nolte"> PMID:8599763</ref> nSH2 was found to interact with the catalytic subunit directly, forming a broad-based scaffold for p110α and coordinates communication between the interacting domains. (Discussed Below). <ref name="Amzel"/>
+<scene name='User:David_Canner/Sandbox_P/Sh2_open/1'>PI3K has two SH2 domains</scene>, an N-terminal (nSH2) domain and a C-terminal (CSH2) domain. <ref name="Flip"/> Both domains recognize similar consensus phosphorylated tyrosine motifs with the pattern: pY-V-X-M in activated receptors and adaptor proteins like PDGF, erbB3, c-Kit and CSF-1 receptors. <ref name="Weber">PMID:11123912</ref> It is upon the interaction of receptor and SH2 domain that the heterodimeric PI3K complex is activated. <ref name="Miled"/> The <scene name='User:David_Canner/Sandbox_P/Sh2/2'>docking site for receptor in NSH2 is defined by the conserved residues Arg 340, Arg 358, and Thr 371</scene> ([[2iui]]), all of which coordinate the phosphorylated tyrosoine phosphate group.<ref name="Nolte"> PMID:8599763</ref> nSH2 was found to interact with the catalytic subunit directly, forming a broad-based scaffold for p110α and coordinates communication between the interacting domains. (Discussed Below). <ref name="Amzel"/>
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