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3aih

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Revision as of 04:01, 5 August 2016

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

Structural highlights

3aih is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1m6p, 1gp0, 1keo, 1q25, 1sz0, 2v5n, 2v5o, 2v5p, 2rl7, 2rl8, 2rl9
Gene:	OS9 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OS9_HUMAN] Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

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.

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang Y, Fu X, Gaiser S, Kottgen M, Kramer-Zucker A, Walz G, Wegierski T. OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum. J Biol Chem. 2007 Dec 14;282(50):36561-70. Epub 2007 Oct 11. PMID:17932042 doi:http://dx.doi.org/10.1074/jbc.M703903200
↑ Christianson JC, Shaler TA, Tyler RE, Kopito RR. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 2008 Mar;10(3):272-82. doi: 10.1038/ncb1689. Epub 2008 Feb 10. PMID:18264092 doi:http://dx.doi.org/10.1038/ncb1689
↑ Bernasconi R, Pertel T, Luban J, Molinari M. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem. 2008 Jun 13;283(24):16446-54. doi: 10.1074/jbc.M802272200. Epub 2008, Apr 15. PMID:18417469 doi:http://dx.doi.org/10.1074/jbc.M802272200
↑ Alcock F, Swanton E. Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. J Mol Biol. 2009 Jan 30;385(4):1032-42. doi: 10.1016/j.jmb.2008.11.045. Epub 2008, Nov 30. PMID:19084021 doi:http://dx.doi.org/10.1016/j.jmb.2008.11.045
↑ Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem. 2009 Jun 19;284(25):17061-8. Epub 2009 Apr 3. PMID:19346256 doi:http://dx.doi.org/M809725200
↑ Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y. Structural Basis for Oligosaccharide Recognition of Misfolded Glycoproteins by OS-9 in ER-Associated Degradation. Mol Cell. 2010 Dec 22;40(6):905-16. PMID:21172656 doi:10.1016/j.molcel.2010.11.017
↑ Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y. Structural Basis for Oligosaccharide Recognition of Misfolded Glycoproteins by OS-9 in ER-Associated Degradation. Mol Cell. 2010 Dec 22;40(6):905-16. PMID:21172656 doi:10.1016/j.molcel.2010.11.017

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3aih"

@@ Line 1: / Line 1: @@
 ==Human OS-9 MRH domain complexed with alpha3,alpha6-Man5==
 <StructureSection load='3aih' size='340' side='right' caption='[[3aih]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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>
 <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 HUMAN])</td></tr>
-<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>
+<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://pdbe.org/3aih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aih RCSB], [http://www.ebi.ac.uk/pdbsum/3aih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aih ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3aih" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3aih

From Proteopedia

Revision as of 04:01, 5 August 2016

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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