Role of the D1-D2 Linker of Human VCP/p97 in the Asymmetry and ATPase Activity of the D1-domain
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep20037.pdf
Reference34 articles.
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2. DeLaBarre, B. & Brunger, A. T. Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat Struc Biol 10, 856–863 (2003).
3. Davies, J. M., Brunger, A. T. & Weis, W. I. Improved Structures of Full-Length p97, an AAA ATPase: Implications for Mechanisms of Nucleotide-Dependent Conformational Change. Structure 16, 715–26 (2008).
4. Huyton, T. et al. The crystal structure of murine p97/VCP at 3.6 Å. J Struc Biol 144, 337–348 (2003).
5. Tang, W. K. et al. A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. Embo J 29, 2217–29 (2010).
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