Hong, Yoon-Hun Ahn, Hee-Chul Lim, Jongsoo Kim, Hong-Man Ji, Hye-Young Lee, Seunga Kim, Ji-Hun Park, Eun Young Song, Hyun Kyu Lee, Bong-Jin 2024-01-20T22:02:41Z 2024-01-20T22:02:41Z 2021-09-03 2009-01-22 0014-5793 https://pubs.kist.re.kr/handle/201004/132793 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. English WILEY STRUCTURAL BASIS INTERACTING MOTIF SIGNAL-TRANSDUCTION CRYSTAL-STRUCTURE CHEMICAL-SHIFT DNA-REPAIR UBA DOMAIN RECOGNITION PROTEINS COMPLEX Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy Article 10.1016/j.febslet.2008.12.034 1 FEBS LETTERS, v.583, no.2, pp.287 - 292 FEBS LETTERS 583 2 287 292 scie scopus 000263101000006 2-s2.0-58149519043 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article STRUCTURAL BASIS INTERACTING MOTIF SIGNAL-TRANSDUCTION CRYSTAL-STRUCTURE CHEMICAL-SHIFT DNA-REPAIR UBA DOMAIN RECOGNITION PROTEINS COMPLEX STAM1 VHS domain Ubiquitin recognition NMR spectroscopy Chemical shift perturbation Protein-protein interaction