Inositol 1,4,5-Trisphosphate Receptor: Difference between revisions

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The InsP<sub>3</sub>R protein can autophosphorylate itself and is a substrate for multiple protein kinases.<ref name="functionref"/>  These kinases include cyclic AMP-dependent protein kinase (PKA), cyclic GMP-dependent protein kinase (PKG) and others.<ref name="functionref"/>  The protein kinases are thought to interact with the InsP<sub>3</sub> receptor by controlling the sensitivity to Ca<sup>2+</sup> in different tissues as well as affecting the sensitivity of InsP<sub>3</sub> itself to Ca<sup>2+</sup>.<ref name="functionref"/>
The InsP<sub>3</sub>R protein can autophosphorylate itself and is a substrate for multiple protein kinases.<ref name="functionref"/>  These kinases include cyclic AMP-dependent protein kinase (PKA), cyclic GMP-dependent protein kinase (PKG) and others.<ref name="functionref"/>  The protein kinases are thought to interact with the InsP<sub>3</sub> receptor by controlling the sensitivity to Ca<sup>2+</sup> in different tissues as well as affecting the sensitivity of InsP<sub>3</sub> itself to Ca<sup>2+</sup>.<ref name="functionref"/>
===3D structures of inositol 1,4,5-trisphosphate receptor===
[[3jrr]] – mInsP3R III ligand-binding suppressor domain – mouse<br />
[[1xzz]] - mInsP3R I ligand-binding suppressor domain<br />
[[1n4k]] - mInsP3R I receptor-binding core + ligand


==References==  
==References==  


<references />
<references />

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Andrea Gorrell, Shannon King, Jaclyn Gordon, David Canner, Michal Harel, Alexander Berchansky, Ann Taylor