User:Alice Harmon/Sandbox 1: Difference between revisions

← Older edit Newer edit →

Revision as of 17:17, 19 August 2013 view source Alice Harmon (talk \| contribs) 392 edits No edit summary ← Older edit		Revision as of 17:27, 19 August 2013 view source Alice Harmon (talk \| contribs) 392 edits No edit summary Newer edit →
Line 36:		Line 36:
	<scene name='55/555705/Subdomainx/1'>Subdomain X</scene> and <scene name='55/555705/Subdomainxi/1'>Subdomain XI</scene> contain three alpha helices (G, H, and I in bovine PKA) that form the kinase core and which are involved in binding substrate proteins.		<scene name='55/555705/Subdomainx/1'>Subdomain X</scene> and <scene name='55/555705/Subdomainxi/1'>Subdomain XI</scene> contain three alpha helices (G, H, and I in bovine PKA) that form the kinase core and which are involved in binding substrate proteins.

	Two hydrophobic spines are composed of amino acid residues that are non-contiguous in the primary structure.<scene name='55/555705/Spine1/1'> Spine 1 </scene>includes the adenine ring of ATP. In PKA the residues are A70, V57, ATP, L173, I174, L172, M128, M231, and L227. Spine two contains residues L106, L95, F185, Y164. Both of these spines are anchored to helix F (Subdomain IX).		Two hydrophobic spines are composed of amino acid residues that are non-contiguous in the primary structure.<scene name='55/555705/Spine1/1'> Spine 1 </scene>includes the adenine ring of ATP. In PKA the residues are A70, V57, ATP, L173, I174, L172, M128, M231, and L227. <scene name='55/555705/Spine2/1'>Spine two</scene> contains residues L106, L95, F185, Y164. Both of these spines are anchored to helix F (Subdomain IX).