Tuesday, July 03, 20122:00 PM - 3:30 PMCNLS Conference Room (TA-3, Bldg 1690)|
q-Bio Seminar Series
Allostery and Conformational Control in Signaling: The Ubiquitin E3 Ligases
Ruth NussinovNational Cancer Institute and Tel Aviv University, Israel
Allostery is important for all cellular events. In E3 ubiquitin ligases, substrate binding proteins, e.g. VHL-box, SOCS-box or the F-box proteins, recruit protein substrates for ubiquitination. Ubiquitination involves several steps. The cullin-RING E3 ligase machinery is involved in one of these. In this step, ubiquitin is transferred from E2 to the substrate protein, labeling the substrate protein for degradation. However, when E3, E3-substrate and E2-ubiquitin crystal structures are modeled together, the distance between the ubiquitinated E2 and the substrate binding site is 50–59 Angstrom, raising the question how the E3 machinery bridges the distance and orients the substrate for the ubiquitin transfer? The talk will address our recent work addressing this fascinating question.
Host: S. Gnanakaran, 5-1923, firstname.lastname@example.org