| Autor: |
Koturenkiene, Agne, Makbul, Cihan, Herrmann, Christian, Constantinescu-Aruxandei, Diana |
| Předmět: |
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| Zdroj: |
Biological Chemistry; May2017, Vol. 398 Issue 5/6, p701-707, 7p, 1 Chart, 2 Graphs |
| Abstrakt: |
Ras-mediated apoptotic signaling is expected to be mediated via Rassf-MST complexes, but the system has been poorly characterized in vitro until now. Here we demonstrate that active H-Ras, Nore1A and MST1 form a stable ternary complex in vitro without other external factors, Nore1A interacting simultaneously with H-Ras and MST1 via its RBD and SARAH domain, respectively. Moreover, our data show for the first time that the SARAH domain of Nore1A plays a role in the Nore1A binding to H-Ras. Finally, we analyze the relation between the electrostatic and hydrophobic forces and kinetic constants of the Nore1A - H-Ras complex. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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