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FEBS Lett. 2009 Jan 22;583(2):287-92. doi: 10.1016/j.febslet.2008.12.034. Epub 2008 Dec 25.

Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy.

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1
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea.

Abstract

Interaction between the signal-transducing adapter molecule 1 (STAM1) Vps27/Hrs/Stam (VHS) domain and ubiquitin was investigated by nuclear magnetic resonance (NMR) spectroscopy. NMR evidence showed that the structure of STAM1 VHS domain resembles that of other VHS domains, especially the homologous domain of STAM2. We found that the VHS domain binds to ubiquitin via its hydrophobic patch consisting of N-terminus of helix 2 and C-terminus of helix 4 in which Trp26 on helix 2 plays a pivotal role in the binding. The binding between VHS and ubiquitin seems to be very similar to that between ubiquitin associated domain (UBA) and ubiquitin, however, the direction of alpha-helices involved in the ubiquitin binding is opposite. Here, we propose a novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain.

PMID:
19111546
DOI:
10.1016/j.febslet.2008.12.034
[Indexed for MEDLINE]
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