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

Title
Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy
Authors
홍윤헌안희철임종수김홍만지혜영이승아김지훈박은영송현규이봉진
Keywords
NMR spectroscopy; protein-protein interaction; STAM1; VHS; STAM1 VHS domain; Ubiquitin recognition; Chemical shift perturbation; Protein?rotein interaction
Issue Date
2009-01
Publisher
FEBS letters
Citation
VOL 583, 287-292
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 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.
URI
http://pubs.kist.re.kr/handle/201004/36122
ISSN
0014-5793
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KIST Publication > Article
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