User:Alice Harmon/Sandbox 2: Difference between revisions
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The crystal structure [[3ku2]] in the right scene shows the inactive 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. | 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. | ||
Revision as of 23:10, 22 August 2013
CDPKCDPK
Calcium-dependent protein kinases (CDPKs) are found in plants, algae, and apicomplexan protists, such as the parasites that cause malaria and toxoplasmosis. They are monomeric enzymes containing an amino-terminal protein kinase domain linked to a carboxy-terminal calcium-binding domain, that has sequence similarity to calmodulin. CDPKs belong to the calmodulin-dependent protein kinase family.
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 [1].
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The crystal structure 3hx4 in the left scene shows the active conformation of the kinase that is bound to calcium (green spheres) and the ATP analog ANP (also called AMPPNP; shown in wireframe and CPK coloring). The catalytic domain is blue and the calcium activation domain (CAD) is gold. In the kinase domain, ANP sits in the catalytic cleft between the large and small lobes of the domain. CAD is bound to the side of the kinase opposite to the catalytic cleft, making it available for peptide substrate binding.
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.
ReferencesReferences
- ↑ Wernimont AK, Artz JD, Finerty P Jr, Lin YH, Amani M, Allali-Hassani A, Senisterra G, Vedadi M, Tempel W, Mackenzie F, Chau I, Lourido S, Sibley LD, Hui R. Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium. Nat Struct Mol Biol. 2010 May;17(5):596-601. Epub 2010 May 2. PMID:20436473 doi:10.1038/nsmb.1795