1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1–Vps60 peptide complex
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Abstract
Vta1 and Vps60 are two ESCRT associated proteins, their direct interaction enhances Vps4 ATPase activity. The N-terminal domain of Vta1 (residues 1–167aa, named as Vta1NTD) contains two tandem MIT domains, which specifically recognize Vps60 and Did2 but not other ESCRT-III subunits. The fragment Vps60 (128–186aa) was reported to display full activity of Vps60, which stimulates Vps4 ATPase in a Vta1-dependent manner. To study the structural basis for the interaction between Vta1 and Vps60, as a first step, here, we report the resonance assignments of the sequential backbone atoms and the side chains of the residues in the two components of Vta1NTD/Vps60128–186 complex at pH 7.0 and 20 °C (BMRB No. 18521).
Keywords
Vta1 Vps60 ESCRT Vps4 MIT domainNotes
Acknowledgments
This work was supported by funding from the National Basic Research Program of China under Nos. 2009CB918600 and 2011CB966300, by National Science Foundation of China Nos. 30970595 and 20921091, and by the International Cooperation Foundation from Science and Technology Commission of Shanghai Municipality under No. 09540703800, and by National New Drug Design Program from Ministry of Health of China under No. 2011ZX09506, and by the funding from State Key laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, CAS, under No. T151102.
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