期刊
JOURNAL OF BIOMOLECULAR NMR
卷 72, 期 1-2, 页码 1-10出版社
SPRINGER
DOI: 10.1007/s10858-018-0201-6
关键词
Endoplasmatic reticulum associated protein degradation; Yos9; Glycan binding; Conformational change
资金
- Deutsche Forschungsgemeinschaft [SFB 740, SFB 1177]
- Center for Biomolecular Magnetic Resonance (BMRZ) at the Goethe University Frankfurt
Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal 1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate receptor homology (MRH) domain of Yos9. We have determined the structure of the MRH domain of Yos9 in its free form and complexed with 3, 6-mannopentaose. We show that binding is achieved by loops between -strands performing an inward movement and that this movement also affects the entire -barrel leading to a twist. These rearrangements may facilitate the processing of client proteins by downstream acting factors. In contrast, other oligosaccharides such as 2-mannobiose bind weakly with only locally occurring chemical shift changes underscoring the specificity of this substrate selection process within ERAD.
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