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3aih

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[[Image:3aih.png|left|200px]]
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==Human OS-9 MRH domain complexed with alpha3,alpha6-Man5==
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<StructureSection load='3aih' size='340' side='right' caption='[[3aih]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3aih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AIH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m6p|1m6p]], [[1gp0|1gp0]], [[1keo|1keo]], [[1q25|1q25]], [[1sz0|1sz0]], [[2v5n|2v5n]], [[2v5o|2v5o]], [[2v5p|2v5p]], [[2rl7|2rl7]], [[2rl8|2rl8]], [[2rl9|2rl9]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OS9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aih RCSB], [http://www.ebi.ac.uk/pdbsum/3aih PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 alpha1,2-linked mannose on C-arm of high-mannose-type glycan and binding of processed alpha1,6-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 alpha3,alpha6-mannopentaose. The OS-9(MRH) has a flattened beta-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 Manalpha1,6Manalpha1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif.
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{{STRUCTURE_3aih| PDB=3aih | SCENE= }}
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Structural Basis for Oligosaccharide Recognition of Misfolded Glycoproteins by OS-9 in ER-Associated Degradation.,Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y Mol Cell. 2010 Dec 22;40(6):905-16. PMID:21172656<ref>PMID:21172656</ref>
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===Human OS-9 MRH domain complexed with alpha3,alpha6-Man5===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_21172656}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3aih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIH OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:021172656</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chen, Y.]]
[[Category: Chen, Y.]]

Revision as of 09:22, 5 November 2014

Human OS-9 MRH domain complexed with alpha3,alpha6-Man5

3aih, resolution 2.10Å

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