Lab Home | Phone | Search
	Center for Nonlinear Studies
	Home  ▶ People   Current   Affiliates   Alumni   Visitors   Students  ▶ Research   ICAM-LANL  ▶ Publications   2007   2006   2005   2004   2003   2002   2001   2000   <1999  ▶ Conferences   Workshops   Sponsorship  ▶ Talks   Colloquia   Seminars   Quantum Lunch   CMS Colloquia   Archive   Kac Lectures   Dist. Quant. Lecture   Ulam Scholar   Colloquia     Jobs  ▶ Students   Summer Research   Graduate Positions  ▶ Visitors   Description  ▶ Services   General   PD Travel Request     History of CNLS     Maps, Directions   CNLS Office   T-Division   LANL				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, ghana@lanl.gov