| http://purl.uniprot.org/citations/21172656 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21172656 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21172656 | http://www.w3.org/2000/01/rdf-schema#comment | "Misfolded glycoproteins are translocated from endoplasmic reticulum (ER) into the cytosol for proteasome-mediated degradation. A mannose-6-phosphate receptor homology (MRH) domain is commonly identified in a variety of proteins and, in the case of OS-9 and XTP3-B, is involved in glycoprotein ER-associated degradation (ERAD). Trimming of outermost α1,2-linked mannose on C-arm of high-mannose-type glycan and binding of processed α1,6-linked mannosyl residues by the MRH domain are critical steps in guiding misfolded glycoproteins to enter ERAD. Here we report the crystal structure of a human OS-9 MRH domain (OS-9(MRH)) complexed with α3,α6-mannopentaose. The OS-9(MRH) has a flattened β-barrel structure with a characteristic P-type lectin fold and possesses distinctive double tryptophan residues in the oligosaccharide-binding site. Our crystallographic result in conjunction with nuclear magnetic resonance (NMR) spectroscopic and biochemical results provides structural insights into the mechanism whereby OS-9 specifically recognizes Manα1,6Manα1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2010.11.017"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2010.11.017"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Satoh T."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Satoh T."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Yamamoto K."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Yamamoto K."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Yamaguchi Y."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Yamaguchi Y."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Hu D."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Hu D."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Hanashima S."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/author | "Hanashima S."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/pages | "905-916"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/pages | "905-916"xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/title | "Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation."xsd:string |
| http://purl.uniprot.org/citations/21172656 | http://purl.uniprot.org/core/title | "Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation."xsd:string |