| Autor: |
Koike, Ryotaro, Ota, Motonori |
| Zdroj: |
Proteins; Jan2024, Vol. 92 Issue 1, p37-43, 7p |
| Abstrakt: |
Capping protein (CP) binds to the barbed end of an actin‐filament and inhibits its elongation. CARMIL binds CP and dissociates it from the barbed end of the actin‐filament. The binding of CARMIL peptide alters the flexibility of CP, which is considered to facilitate the dissociation. Twinfilin also binds to CP through its C‐terminal tail. The complex structures of the CP/twinfilin‐tail (TW‐tail) peptide indicate that the binding sites of CARMIL and TW‐tail overlap. However, TW‐tail binding does not facilitate the dissociation of CP from the barbed end. We extensively investigated the flexibilities of CP in the CP/TW‐tail or CP/CARMIL complexes using an elastic network model and concluded that TW‐tail binding does not alter the flexibility of CP. Our extensive analysis also highlighted that the strong contacts of peptides with the two domains of CP, that is, the CP‐L and CP‐S domains, are key to changing the flexibilities of CP. CARMIL peptides can interact strongly with both of the domains, while TW‐tail peptides exclusively interact with the CP‐S domain because the binding site of TW‐tail on CP relatively shifts to the CP‐S domain compared with that of CP/CARMIL. This result supports our hypothesis that the dissociation of CP from the barbed end is regulated by the flexibility of CP. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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