Sandbox 154: Difference between revisions
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==== Stability ==== | ==== Stability ==== | ||
The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge</scene> | The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge formations</scene> involving arginine 206, 183, 177 (purple); glutamate 72(blue), aspartate 187(green), 179 and 4-methyl histidine 73(yellow). Additional stability is believed to arise from a break in the interaction between residues <scene name='Sandbox_154/2zwh_leu_val/2'>108-111 and Val165 and Ile175</scene> in the same half of their respective domains to a new interaction between <scene name='Sandbox_154/2zwh_leu_thr/2'>Leu110 and Thr194</scene> where a much greater distance is observed between them<ref name="oda" />. | ||
Once the P<sub>i</sub> is released, a conformational change on the D-loop results in the “softening” of the F-actin filament. That is, it makes the ADP-actin monomer more unstable and makes it more susceptible to cleavage <ref name=”Pfaedtner2”>PMID: 19931282</ref> | Once the P<sub>i</sub> is released, a conformational change on the D-loop results in the “softening” of the F-actin filament. That is, it makes the ADP-actin monomer more unstable and makes it more susceptible to cleavage <ref name=”Pfaedtner2”>PMID: 19931282</ref> | ||
