User:Alice Harmon/Sandbox 2: Difference between revisions

Line 5:

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 Ca<sup>2+</sup> to the regulatory domain (called the calcium activation domain or CAD), which contains four [[EF hand]] calcium-binding sites. CDPKs are thus are activated by processes that elevate the concentration of calcium inside cells.

Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the conformation changes that occur upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>. Not only is the internal structures of each domain affected, but also the site of interaction of the two domains is completely different. For comparison see [[Eukaryotic Protein Kinase Catalytic Domain]] and [[EF-hand]] for a guides to their structures.

Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the conformation changes that occur upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>. To view compare the two structures click on pairs of green links that have the same number.

Not only is the internal structures of each domain affected, but also the site of interaction of the two domains is completely different. For comparison see [[Eukaryotic Protein Kinase Catalytic Domain]] and [[EF-hand]] for a guides to their structures.

@@ Line 5: / Line 5: @@
 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 Ca<sup>2+</sup> to the regulatory domain (called the calcium activation domain or CAD), which contains four [[EF hand]] calcium-binding sites. CDPKs are thus are activated by processes that elevate the concentration of calcium inside cells.
-Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the  conformation changes that occur upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>. Not only is the internal structures of each domain affected, but also the site of interaction of the two domains is completely different. For comparison see [[Eukaryotic Protein Kinase Catalytic Domain]] and [[EF-hand]] for a guides to their structures.
+Crystal structures of inactive and active conformations of CDPK1 from ''Toxoplasma gondii'' show the conformation changes that occur upon the binding of calcium to the regulatory domain <ref> PMID:20436473 </ref>. To view compare the two structures click on pairs of green links that have the same number.
+Not only is the internal structures of each domain affected, but also the site of interaction of the two domains is completely different. For comparison see [[Eukaryotic Protein Kinase Catalytic Domain]] and [[EF-hand]] for a guides to their structures.