User:Alice Harmon/Sandbox 2: Difference between revisions

Line 13:

The crystal structure [[3hx4]] in the left scene shows the ~~<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. 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 [[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 ~~<scene name='55/559103/Holo-ikinase/1'>~~inactive ~~conformation</scene>~~ 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 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 23:00, 22 August 2013 view source Alice Harmon (talk \| contribs) 392 edits No edit summary ← Older edit		Revision as of 23:09, 22 August 2013 view source Alice Harmon (talk \| contribs) 392 edits No edit summary Newer edit →
Line 13:		Line 13:


	The crystal structure [[3hx4]] in the left scene shows the ~~<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. 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 [[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 ~~<scene name='55/559103/Holo-ikinase/1'>~~inactive ~~conformation</scene>~~ 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 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.