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)

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 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
Volume583
Issue number2
DOIs
Publication statusPublished - 2009 Jan 22

Bibliographical note

Funding Information:
We thank the staff at the KIST 900 MHz NMR facility. This work was supported by a grant from the Basic Research Program of Korea Science and Engineering Foundation (R01-2004-000-10773-0). This work was also supported in part by the 2007 BK21 project for Medicine, Dentistry and Pharmacy, and by Grant 2Z03130 from Korea Institute of Science and Technology, Korea.

Keywords

  • 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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