Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding.
Monoubiquitination serves as a regulatory signal in a variety of cellular processes. Monoubiquitin signals are transmitted by binding to a small but rapidly expanding class of ubiquitin binding motifs. Several of these motifs, including the CUE domain, also promote intramolecular monoubiquitination. The solution structure of a CUE domain of the ... yeast Cue2 protein in complex with ubiquitin reveals intermolecular interactions involving conserved hydrophobic surfaces, including the Leu8-Ile44-Val70 patch on ubiquitin. The contact surface extends beyond this patch and encompasses Lys48, a site of polyubiquitin chain formation. This suggests an occlusion mechanism for inhibiting polyubiquitin chain formation during monoubiquitin signaling. The CUE domain shares a similar overall architecture with the UBA domain, which also contains a conserved hydrophobic patch. Comparative modeling suggests that the UBA domain interacts analogously with ubiquitin. The structure of the CUE-ubiquitin complex may thus serve as a paradigm for ubiquitin recognition and signaling by ubiquitin binding proteins.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Carrier Proteins, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin
Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Carrier Proteins, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin
Cell
Date: May. 30, 2003
PubMed ID: 12787503
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