User:Alice Harmon/Sandbox 2: Difference between revisions

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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>.
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>.


<Structure load='3HX4' size='500' frame='true' align='right' caption='TgCDPK1 scene = '55/559103/Holo-akinase/1' />
<Structure load='3HX4' size='500' frame='true' align='left' caption='active TgCDPK1' scene = '55/559103/Holo-akinase/1' />
<Structure load='3HX4' size='500' frame='true' align='right' caption='inactive TgCDPK1' scene = '55/559103/Holo-ikinase/1' />


The crystal structure [[3hx4]] shows that <scene name='55/559103/Holo-akinase/1'>active conformation</scene> 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. Note that CAD is bound to the side of the kinase that is opposite of the catalytic cleft, making it available for peptide substrate binding.
The crystal structure [[3hx4]] shows that <scene name='55/559103/Holo-akinase/1'>active conformation</scene> 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. Note that CAD is bound to the side of the kinase that is opposite of the catalytic cleft, making it available for peptide substrate binding.