User:Peyton Jenkins/Sandbox 1
From Proteopedia
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== Structural Highlights == | == Structural Highlights == | ||
=== STK11 === | === STK11 === | ||
| - | [[STK11]] can be broken down into 3 domains. An N-terminal domain (aa 1-42), kinase domain (aa 43-347), and a C-terminal domain (aa 348-433). The <scene name='10/1078094/Active_site/1'>activation loop</scene> of [[STK11]] is located from residues ~202-212. Within the activation loop is F204, which interacts with a hydrophobic pocket on MO25, which is necessary to stabilize the active conformation. Within the αC helix is residue D98 which forms a <scene name='10/1078094/78and98/2'>salt bridge</scene> with K78, further stabilizing the active site and aids in ATP binding. Mg<sup>2+</sup> helps aid ATP binding, however in this structure there is a point mutation (<scene name='10/1078094/D194a/1'>D194A</scene>) to make STK11 catalytically inactive. Another loop, the <scene name='10/1078094/B2b3_loop/ | + | [[STK11]] can be broken down into 3 domains. An N-terminal domain (aa 1-42), kinase domain (aa 43-347), and a C-terminal domain (aa 348-433). The <scene name='10/1078094/Active_site/1'>activation loop</scene> of [[STK11]] is located from residues ~202-212. Within the activation loop is F204, which interacts with a hydrophobic pocket on MO25, which is necessary to stabilize the active conformation. Within the αC helix is residue D98 which forms a <scene name='10/1078094/78and98/2'>salt bridge</scene> with K78, further stabilizing the active site and aids in ATP binding. Mg<sup>2+</sup> helps aid ATP binding, however in this structure there is a point mutation (<scene name='10/1078094/D194a/1'>D194A</scene>) to make STK11 catalytically inactive. Another loop, the <scene name='10/1078094/B2b3_loop/2'>β2-β3 loop</scene> is essential for binding of STRADα on the N-terminal lobe of STK11. β7-β8 sheets of STK11 also interact with STRADα. In the β2-β3 loop R74 hydrogen bonds with Q251 of STRADα. |
=== STRADα === | === STRADα === | ||
STRAD alpha is composed of 2 domains, an N-terminal domain (aa 1-58) and pseudokinase domain (aa 59-347). STRADα is termed a pseudokinase because it shares structural features, such as a p+1 loop and αG helix, with other kinases, but lacks catalytic activity. STRADα binds STK11 through its pseudokinase domain, with the activation loop interacting with the the β2-β3 loop and β7-β8 sheets of STK11. The αC of STRADα interacts with the surface of MO25, further stabilizing the interaction between proteins. Additionally there is a WEF motif (aa 429-431) on the C-terminus of STRADα interacting with the C-terminus of MO25. | STRAD alpha is composed of 2 domains, an N-terminal domain (aa 1-58) and pseudokinase domain (aa 59-347). STRADα is termed a pseudokinase because it shares structural features, such as a p+1 loop and αG helix, with other kinases, but lacks catalytic activity. STRADα binds STK11 through its pseudokinase domain, with the activation loop interacting with the the β2-β3 loop and β7-β8 sheets of STK11. The αC of STRADα interacts with the surface of MO25, further stabilizing the interaction between proteins. Additionally there is a WEF motif (aa 429-431) on the C-terminus of STRADα interacting with the C-terminus of MO25. | ||
Revision as of 22:20, 29 April 2025
β==2WTK: Hetertrimeric Complex of STK11, MO25, and STRADα==
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