Abstract
The X-ray structure at 2.0-Å resolution of the p90 ribosomal S6 kinase 2 C-terminal kinase domain revealed a C-terminal autoinhibitory αL-helix that was embedded in the kinase scaffold and determines the inactive kinase conformation. We suggest a mechanism of activation through displacement of the αL-helix and rearrangement of the conserved residue Glu500, as well as the reorganization of the T-loop into the active conformation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 112-113 |
| Number of pages | 2 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 15 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2008 |
Bibliographical note
Funding Information:Use of the Advanced Photon Source was supported by the US Department of Energy, Office of Basic Energy Sciences, under contract DE-AC02-06CH11357. Part of this work was conducted at the Northeastern Collaborative Access Team, Sector 24-ID, supported by award RR-15301 from the US National Center for Research Resources at the National Institutes of Health. Use of the General Medicine and Cancer Institutes Collaborative Access Team Sector 23-ID was funded with federal funds from the US National Cancer Institute (Y1-CO-1020) and National Institute of General Medical Science (Y1-GM-1104). Other funding was provided by The Hormel Foundation and US National Institutes of Health grants CA111356, CA111536, CA077646, CA081064 and CA120388.