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| | <StructureSection load='5ao6' size='340' side='right'caption='[[5ao6]], [[Resolution|resolution]] 3.36Å' scene=''> | | <StructureSection load='5ao6' size='340' side='right'caption='[[5ao6]], [[Resolution|resolution]] 3.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ao6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AO6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ao6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AO6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ao5|5ao5]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ao6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ao6 OCA], [https://pdbe.org/5ao6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ao6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ao6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ao6 ProSAT]</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=5ao6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ao6 OCA], [http://pdbe.org/5ao6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ao6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ao6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ao6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MRC2_HUMAN MRC2_HUMAN]] May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).<ref>PMID:10683150</ref> <ref>PMID:12972549</ref> | + | [https://www.uniprot.org/uniprot/MRC2_HUMAN MRC2_HUMAN] May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).<ref>PMID:10683150</ref> <ref>PMID:12972549</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Briggs, D C]] | + | [[Category: Briggs DC]] |
| - | [[Category: Carafoli, F]] | + | [[Category: Carafoli F]] |
| - | [[Category: Hohenester, E]] | + | [[Category: Hohenester E]] |
| - | [[Category: Loncar, T]] | + | [[Category: Loncar T]] |
| - | [[Category: Paracuellos, P]] | + | [[Category: Paracuellos P]] |
| - | [[Category: C-type lectin domain]]
| + | |
| - | [[Category: Collagen]]
| + | |
| - | [[Category: Endocytic receptor]]
| + | |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: Fibronectin type ii domain]]
| + | |
| - | [[Category: Gelatin]]
| + | |
| Structural highlights
Function
MRC2_HUMAN May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).[1] [2]
Publication Abstract from PubMed
The C-type mannose receptor and its homolog Endo180 (or uPARAP, for urokinase plasminogen activator receptor-associated protein) mediate the endocytic uptake of collagen by macrophages and fibroblasts. This process is required for normal tissue remodeling, but also facilitates the growth and dissemination of tumors. We have determined the crystal structure at 2.5 A resolution of the N-terminal region of Endo180, consisting of a ricin-like domain, a fibronectin type II (FN2) domain, and two C-type lectin (CTL) domains. The L-shaped arrangement of these domains creates a shallow trench spanning the FN2 and CTL1 domains, which was shown by mutagenesis to bind triple-helical and denatured collagen. Small-angle X-ray scattering showed that the L-shaped structure is maintained in solution at neutral and acidic pH, irrespective of calcium ion loading. Collagen binding was equally unaffected by acidic pH, suggesting that collagen release in endosomes is not regulated by changes within the Endo180 N-terminal region.
Insights into Collagen Uptake by C-type Mannose Receptors from the Crystal Structure of Endo180 Domains 1-4.,Paracuellos P, Briggs DC, Carafoli F, Loncar T, Hohenester E Structure. 2015 Nov 3;23(11):2133-42. doi: 10.1016/j.str.2015.09.004. Epub 2015, Oct 15. PMID:26481812[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sheikh H, Yarwood H, Ashworth A, Isacke CM. Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor. J Cell Sci. 2000 Mar;113 ( Pt 6):1021-32. PMID:10683150
- ↑ Wienke D, MacFadyen JR, Isacke CM. Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor. Mol Biol Cell. 2003 Sep;14(9):3592-604. Epub 2003 Jul 25. PMID:12972549 doi:http://dx.doi.org/10.1091/mbc.E02-12-0814
- ↑ Paracuellos P, Briggs DC, Carafoli F, Loncar T, Hohenester E. Insights into Collagen Uptake by C-type Mannose Receptors from the Crystal Structure of Endo180 Domains 1-4. Structure. 2015 Nov 3;23(11):2133-42. doi: 10.1016/j.str.2015.09.004. Epub 2015, Oct 15. PMID:26481812 doi:http://dx.doi.org/10.1016/j.str.2015.09.004
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