User:Nathan Roy: Difference between revisions

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When MA is not bound to PI(4,5)P2 (Figure 1), notice the alignment of helix 1, and more precisely, the orientation of Leu 8 and Glu 12.<scene name='User:Nathan_Roy/Unbound_residues/2'>~~TextToBeDisplayed~~</scene>. In this PI(4,5)P2 unbound structure, the myristyl group is sequestered in the pocket of helix 1 created by Leu 8 and Glu 12. Upon binding of PI(4,5)P2 to the hydrophobic groove created by helix 2, a type 2 beta turn, and helix 5, a slight conformational switch occurs in helix 1 (Figure 2), <applet load='2H3Q_mono1.pdb' size='300' frame='true' align='left' caption='FIGURE 2. MA bound to PI(4,5)P2' /> causing a change in the alignment of Leu 8 and Glu 12,(<scene name='User:Nathan_Roy/Myr_out/2'>~~TextToBeDisplayed~~</scene>) ejecting the myristyl group from it's sequestered state. This structural switch allows membrane anchoring to be directly coupled to proper membrane localization of Gag, and thus efficient particle release.

When MA is not bound to PI(4,5)P2 (Figure 1), notice the alignment of helix 1, and more precisely, the orientation of Leu 8 and Glu 12(<scene name='User:Nathan_Roy/Unbound_residues/2'>Show Residues</scene>). In this PI(4,5)P2 unbound structure, the myristyl group is sequestered in the pocket of helix 1 created by Leu 8 and Glu 12. Upon binding of PI(4,5)P2 to the hydrophobic groove created by helix 2, a type 2 beta turn, and helix 5, a slight conformational switch occurs in helix 1 (Figure 2), <applet load='2H3Q_mono1.pdb' size='300' frame='true' align='left' caption='FIGURE 2. MA bound to PI(4,5)P2' /> causing a change in the alignment of Leu 8 and Glu 12,(<scene name='User:Nathan_Roy/Myr_out/2'>Show Residues</scene>) ejecting the myristyl group from it's sequestered state. This structural switch allows membrane anchoring to be directly coupled to proper membrane localization of Gag, and thus efficient particle release.

User:Nathan Roy: Difference between revisions

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Revision as of 15:11, 21 April 2009 view source Nathan Roy (talk \| contribs) 76 edits No edit summary ← Older edit		Revision as of 17:05, 21 April 2009 view source Nathan Roy (talk \| contribs) 76 edits No edit summary Newer edit →
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	When MA is not bound to PI(4,5)P2 (Figure 1), notice the alignment of helix 1, and more precisely, the orientation of Leu 8 and Glu 12.<scene name='User:Nathan_Roy/Unbound_residues/2'>~~TextToBeDisplayed~~</scene>. In this PI(4,5)P2 unbound structure, the myristyl group is sequestered in the pocket of helix 1 created by Leu 8 and Glu 12. Upon binding of PI(4,5)P2 to the hydrophobic groove created by helix 2, a type 2 beta turn, and helix 5, a slight conformational switch occurs in helix 1 (Figure 2), <applet load='2H3Q_mono1.pdb' size='300' frame='true' align='left' caption='FIGURE 2. MA bound to PI(4,5)P2' /> causing a change in the alignment of Leu 8 and Glu 12,(<scene name='User:Nathan_Roy/Myr_out/2'>~~TextToBeDisplayed~~</scene>) ejecting the myristyl group from it's sequestered state. This structural switch allows membrane anchoring to be directly coupled to proper membrane localization of Gag, and thus efficient particle release.		When MA is not bound to PI(4,5)P2 (Figure 1), notice the alignment of helix 1, and more precisely, the orientation of Leu 8 and Glu 12(<scene name='User:Nathan_Roy/Unbound_residues/2'>Show Residues</scene>). In this PI(4,5)P2 unbound structure, the myristyl group is sequestered in the pocket of helix 1 created by Leu 8 and Glu 12. Upon binding of PI(4,5)P2 to the hydrophobic groove created by helix 2, a type 2 beta turn, and helix 5, a slight conformational switch occurs in helix 1 (Figure 2), <applet load='2H3Q_mono1.pdb' size='300' frame='true' align='left' caption='FIGURE 2. MA bound to PI(4,5)P2' /> causing a change in the alignment of Leu 8 and Glu 12,(<scene name='User:Nathan_Roy/Myr_out/2'>Show Residues</scene>) ejecting the myristyl group from it's sequestered state. This structural switch allows membrane anchoring to be directly coupled to proper membrane localization of Gag, and thus efficient particle release.