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| | <StructureSection load='1o91' size='340' side='right'caption='[[1o91]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1o91' size='340' side='right'caption='[[1o91]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o91]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o91]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O91 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1o91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o91 OCA], [http://pdbe.org/1o91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o91 RCSB], [http://www.ebi.ac.uk/pdbsum/1o91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o91 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1o91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o91 OCA], [https://pdbe.org/1o91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o91 RCSB], [https://www.ebi.ac.uk/pdbsum/1o91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o91 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CO8A1_MOUSE CO8A1_MOUSE] Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis.<ref>PMID:15063777</ref> <ref>PMID:16269661</ref> <ref>PMID:19401424</ref> Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Bogin, O]] | + | [[Category: Bogin O]] |
| - | [[Category: Hohenester, E]] | + | [[Category: Hohenester E]] |
| - | [[Category: Kvansakul, M]] | + | [[Category: Kvansakul M]] |
| - | [[Category: Yayon, A]] | + | [[Category: Yayon A]] |
| - | [[Category: Adhesion]]
| + | |
| - | [[Category: C1q_like_domain]]
| + | |
| - | [[Category: Collagen]]
| + | |
| - | [[Category: Connective tissue]]
| + | |
| - | [[Category: Extracellular matrix]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
CO8A1_MOUSE Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis.[1] [2] [3] Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Collagen VIII is a major component of Descemet's membrane and is also found in vascular subendothelial matrices. The C-terminal non-collagenous domain (NC1) domain of collagen VIII, which is a member of the C1q-like protein family, forms a stable trimer and is thought to direct the assembly of the collagen triple helix, as well as polygonal supramolecular structures. We have solved the crystal structure of the mouse alpha1(VIII)(3) NC1 domain trimer at 1.9 A resolution. Each subunit of the intimate NC1 trimer consists of a ten-stranded beta-sandwich. The surface of the collagen VIII NC1 trimer presents three strips of partially exposed aromatic residues shown to interact with the non-ionic detergent CHAPS, which are likely to be involved in supramolecular assemblies. Equivalent strips exist in the NC1 domain of the closely related collagen X, suggesting a conserved assembly mechanism. Surprisingly, the collagen VIII NC1 trimer lacks the buried calcium cluster of the collagen X NC1 trimer. The mouse alpha1(VIII) and alpha2(VIII) NC1 domains are 71.5% identical in sequence, with the differences being concentrated on the NC1 trimer surface. A few non-conservative substitutions map to the subunit interfaces near the surface, but it is not obvious from the structure to what extent they determine the preferred assembly of collagen VIII alpha1 and alpha2 chains into homotrimers.
Crystal structure of the collagen alpha1(VIII) NC1 trimer.,Kvansakul M, Bogin O, Hohenester E, Yayon A Matrix Biol. 2003 Apr;22(2):145-52. PMID:12782141[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hirano S, Yonezawa T, Hasegawa H, Hattori S, Greenhill NS, Davis PF, Sage EH, Ninomiya Y. Astrocytes express type VIII collagen during the repair process of brain cold injury. Biochem Biophys Res Commun. 2004 Apr 30;317(2):437-43. PMID:15063777 doi:10.1016/j.bbrc.2004.03.049
- ↑ Adiguzel E, Hou G, Mulholland D, Hopfer U, Fukai N, Olsen B, Bendeck M. Migration and growth are attenuated in vascular smooth muscle cells with type VIII collagen-null alleles. Arterioscler Thromb Vasc Biol. 2006 Jan;26(1):56-61. PMID:16269661 doi:10.1161/01.ATV.0000194155.96456.b7
- ↑ Hopfer U, Hopfer H, Meyer-Schwesinger C, Loeffler I, Fukai N, Olsen BR, Stahl RA, Wolf G. Lack of type VIII collagen in mice ameliorates diabetic nephropathy. Diabetes. 2009 Jul;58(7):1672-81. PMID:19401424 doi:10.2337/db08-0183
- ↑ Kvansakul M, Bogin O, Hohenester E, Yayon A. Crystal structure of the collagen alpha1(VIII) NC1 trimer. Matrix Biol. 2003 Apr;22(2):145-52. PMID:12782141
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