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Biomol NMR Assign. 2013 Oct;7(2):331-4. doi: 10.1007/s12104-012-9439-1. Epub 2012 Nov 7.

¹H, ¹³C and ¹⁵N resonance assignments of the N-terminal domain of Vta1-Vps60 peptide complex.

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  • 1State Key Laboratory of Natural Products and Bioorganic Chemistry, Shanghai Institute of Organic Chemistry, CAS, 345 Lingling Rd., Shanghai 200032, China.


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/Vps60(128-186) complex at pH 7.0 and 20 °C (BMRB No. 18521).

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