User:Alice Harmon/Sandbox 2: Difference between revisions

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==CDPK==

Calcium-dependent protein kinases (CDPKs) are found in plants, green algae, and protists. In plants CDPKs are encoded by large gene families<ref> ~~PMCID~~:~~PMC167006~~</ref><ref>PMID:~~17172291~~</ref> and they are involved in many cellular responses to stimuli such as hormones. In the apicomplexan protists ''Plasmodium falciparum''(parasite that causes malaria) and ''Toxoplasma gondii''(parasite that causes toxoplasmosis), CDPKs are encoded by small gene families and they are involved in critical stages of the parasite life cycle <ref>~~PMCID~~:~~PMC3514314~~</ref><ref>PMID:20466936.

Calcium-dependent protein kinases (CDPKs) are found in plants, green algae, and protists. In plants CDPKs are encoded by large gene families<ref> PMID:12805596</ref><ref>PMID:15695435</ref> and they are involved in many cellular responses to stimuli such as hormones . In the apicomplexan protists ''Plasmodium falciparum''(parasite that causes malaria) and ''Toxoplasma gondii''(parasite that causes toxoplasmosis), CDPKs are encoded by small gene families, and they are involved in critical stages of the parasite life cycle <ref>PMID:23226109</ref><ref>PMID:20466936</ref>.

CDPKs are monomeric enzymes containing an amino-terminal protein kinase domain linked to a carboxy-terminal calcium-binding regulatory domain, which has sequence similarity to calmodulin, and they belong to the calmodulin-dependent protein kinase family<ref>~~PMCID~~:1852075</ref>. CDPKs are regulated by the binding of calcium to the regulatory domain, and thus are activated in processes that elevate the concentration of calcium inside cells.

CDPKs are monomeric enzymes containing an amino-terminal protein kinase domain linked to a carboxy-terminal calcium-binding regulatory domain, which has sequence similarity to calmodulin, and they belong to the calmodulin-dependent protein kinase family<ref>PMID:1852075</ref>. CDPKs are regulated by the binding of calcium to the regulatory domain, and thus are activated in processes that elevate the concentration of calcium inside cells.

Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the dramatic conformation change that occurs upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>.

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|The crystal structure [[3ku2]] in the right scene shows the '''inactive conformation''' of the kinase that is bound only to the ANP (wireframe and CPK coloring). As above, the catalytic domain is blue and the CAD is gold. The large lobe of the kinase domain is in approximately the same orientation as in the left scene. Note the large conformational change in the CAD (long alpha helices) and that it is now bound to the same side of the kinase as the catalytic cleft (marked by the bound ANP), blocking it from binding peptide substrate.

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=References=

==References==

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 ==CDPK==
-Calcium-dependent protein kinases (CDPKs) are found in plants, green algae, and protists. In plants CDPKs are encoded by large gene families<ref> PMCID:PMC167006</ref><ref>PMID:17172291</ref> and they are involved in many cellular responses to stimuli such as hormones. In the apicomplexan protists ''Plasmodium falciparum''(parasite that causes malaria) and ''Toxoplasma gondii''(parasite that causes toxoplasmosis), CDPKs are encoded by small gene families and they are involved in critical stages of the parasite life cycle <ref>PMCID:PMC3514314</ref><ref>PMID:20466936.
+Calcium-dependent protein kinases (CDPKs) are found in plants, green algae, and protists. In plants CDPKs are encoded by large gene families<ref> PMID:12805596</ref><ref>PMID:15695435</ref> and they are involved in many cellular responses to stimuli such as hormones . In the apicomplexan protists ''Plasmodium falciparum''(parasite that causes malaria) and ''Toxoplasma gondii''(parasite that causes toxoplasmosis), CDPKs are encoded by small gene families, and they are involved in critical stages of the parasite life cycle <ref>PMID:23226109</ref><ref>PMID:20466936</ref>.
-CDPKs are monomeric enzymes containing an amino-terminal protein kinase domain linked to a carboxy-terminal calcium-binding regulatory domain, which has sequence similarity to calmodulin, and they belong to the calmodulin-dependent protein kinase family<ref>PMCID:1852075</ref>. CDPKs are regulated by the binding of calcium to the regulatory domain, and thus are activated in processes that elevate the concentration of calcium inside cells.
+CDPKs are monomeric enzymes containing an amino-terminal protein kinase domain linked to a carboxy-terminal calcium-binding regulatory domain, which has sequence similarity to calmodulin, and they belong to the calmodulin-dependent protein kinase family<ref>PMID:1852075</ref>. CDPKs are regulated by the binding of calcium to the regulatory domain, and thus are activated in processes that elevate the concentration of calcium inside cells.
 Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the dramatic conformation change that occurs upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>.
@@ Line 17: / Line 17: @@
 |The crystal structure [[3ku2]] in the right scene shows the '''inactive conformation''' of the kinase that is bound only to the ANP (wireframe and CPK coloring). As above, the catalytic domain is blue and the CAD is gold. The large lobe of the kinase domain is in approximately the same orientation as in the left scene. Note the large conformational change in the CAD (long alpha helices) and that it is now bound to the same side of the kinase as the catalytic cleft (marked by the bound ANP), blocking it from binding peptide substrate.
 |}
+=References=
+<references/>
 ==References==
 <references/>