Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation-Reference-Cited by-同舟云学术

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Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation

Published:2014-12-01 Issue:1 Volume:22 Page:37-43
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Thevakumaran Neroshan,Lavoie Hugo,Critton David A,Tebben Andrew,Marinier Anne,Sicheri Frank,Therrien Marc

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2924.pdf

Reference34 articles.

1. Rajakulendran, T., Sahmi, M., Lefrancois, M., Sicheri, F. & Therrien, M. A dimerization-dependent mechanism drives RAF catalytic activation. Nature 461, 542–545 (2009).

2. Zhang, B.H. & Guan, K.L. Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601. EMBO J. 19, 5429–5439 (2000).

3. Chong, H., Lee, J. & Guan, K.L. Positive and negative regulation of Raf kinase activity and function by phosphorylation. EMBO J. 20, 3716–3727 (2001).

4. Freeman, A.K., Ritt, D.A. & Morrison, D.K. Effects of Raf dimerization and its inhibition on normal and disease-associated Raf signaling. Mol. Cell 49, 751–758 (2013).

5. Wan, P.T. et al. Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 116, 855–867 (2004).

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