Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy.
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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Binding Sites, Endosomal Sorting Complexes Required for Transport, Humans, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Phosphoproteins, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Structure, Secondary, Tryptophan, Ubiquitin
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Binding Sites, Endosomal Sorting Complexes Required for Transport, Humans, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Phosphoproteins, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Structure, Secondary, Tryptophan, Ubiquitin
FEBS Lett.
Date: Jan. 22, 2009
PubMed ID: 19111546
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