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

Yoon Hun Hong, Hee Chul Ahn, Jongsoo Lim, Hong Man Kim, Hye Young Ji, Seunga Lee, Ji Hun Kim, Eun Young Park, Hyun Kyu Song, Bong Jin Lee

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


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 α-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. Structured summary: MINT-6804185:. STAM1 (uniprotkb:Q92783) binds (MI:0407) to ubiquitin (uniprotkb:P62988) by nuclear magnetic resonance (MI:0077).

Original languageEnglish
Pages (from-to)287-292
Number of pages6
JournalFEBS Letters
Issue number2
Publication statusPublished - 2009 Jan 22


  • Chemical shift perturbation
  • NMR spectroscopy
  • Protein-protein interaction
  • STAM1 VHS domain
  • Ubiquitin recognition

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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