Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy
- Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy
- 홍윤헌; 안희철; 임종수; 김홍만; 지혜영; 이승아; 김지훈; 박은영; 송현규; 이봉진
- NMR spectroscopy; protein-protein interaction; STAM1; VHS; STAM1 VHS domain; Ubiquitin recognition; Chemical shift perturbation; Protein？rotein interaction
- Issue Date
- FEBS letters
- VOL 583, 287-292
- 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 a-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.
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