Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 1, Pages 112-113Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1347
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Funding
- NCI NIH HHS [R37 CA081064, Y01 CO1020-11, CA120388, R01 CA077646, R01 CA111536, CA081064, Y1-CO-1020, R01 CA077646-10, R01 CA111356, R01 CA081064, CA111536, R01 CA111356-03, R01 CA120388, CA077646, R01 CA081064-08, CA111356, R01 CA111536-05, R01 CA120388-05] Funding Source: Medline
- NCRR NIH HHS [RR-15301, P41 RR015301, P41 RR015301-05] Funding Source: Medline
- NIGMS NIH HHS [Y1-GM-1104, Y01 GM1104-11] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA111356, R01CA120388, R01CA111536, R01CA077646, R37CA081064, R01CA081064] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR015301] Funding Source: NIH RePORTER
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The X-ray structure at 2.0-angstrom resolution of the p90 ribosomal S6 kinase 2 C-terminal kinase domain revealed a C-terminal autoinhibitory alpha L-helix that was embedded in the kinase scaffold and determines the inactive kinase conformation. We suggest a mechanism of activation through displacement of the alpha L-helix and rearrangement of the conserved residue Glu500, as well as the reorganization of the T-loop into the active conformation.
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