These authors contributed equally.
Structural and mechanistic insights into Mps1 kinase activation
Article first published online: 16 DEC 2008
© 2008 The Authors Journal compilation © 2009 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd
Journal of Cellular and Molecular Medicine
Volume 13, Issue 8b, pages 1679–1694, August 2009
How to Cite
Wang, W., Yang, Y., Gao, Y., Xu, Q., Wang, F., Zhu, S., Old, W., Resing, K., Ahn, N., Lei, M. and Liu, X. (2009), Structural and mechanistic insights into Mps1 kinase activation. Journal of Cellular and Molecular Medicine, 13: 1679–1694. doi: 10.1111/j.1582-4934.2008.00605.x
- Issue published online: 26 NOV 2009
- Article first published online: 16 DEC 2008
- Received: July 18, 2008; Accepted: October 29, 2008
Figure S1. The inhibited ATP-binding site of Pak1. The kinase inhibitory (KI) segment of the autoregulatory fragment occupies the cleft between the small and the large lobes of the kinase domain. Lys141 makes hydrogen bonds with Asp407 of the activation loop. Therefore, the activation loop is forced to make a turn, which blocks the contact between Glu355 of Helix C and Lys299Arg and prevents binding of ATP. The hydrogen bonding interactions are shown as magenta-dotted lines.
Please note: Wiley-Blackwell are not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article.
|JCMM_605_sm_fS1.ppt||418K||Supporting info item|
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.