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| | ==Crystal structure of the Collagen VI alpha3 N5 domain R1061Q== | | ==Crystal structure of the Collagen VI alpha3 N5 domain R1061Q== |
| - | <StructureSection load='4ihk' size='340' side='right' caption='[[4ihk]], [[Resolution|resolution]] 1.20Å' scene=''> | + | <StructureSection load='4ihk' size='340' side='right'caption='[[4ihk]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ihk]] is a 1 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=4IHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IHK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ihk]] is a 1 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=4IHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4igi|4igi]]</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=4ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihk OCA], [https://pdbe.org/4ihk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihk RCSB], [https://www.ebi.ac.uk/pdbsum/4ihk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Col6a3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihk OCA], [http://pdbe.org/4ihk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ihk RCSB], [http://www.ebi.ac.uk/pdbsum/4ihk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E9PWQ3_MOUSE E9PWQ3_MOUSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Collagen|Collagen]] | + | *[[Collagen 3D structures|Collagen 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Becker, A K.A]] | + | [[Category: Mus musculus]] |
| - | [[Category: Mikolajek, H]] | + | [[Category: Becker AKA]] |
| - | [[Category: Paulsson, M]] | + | [[Category: Mikolajek H]] |
| - | [[Category: Wagener, R]] | + | [[Category: Paulsson M]] |
| - | [[Category: Werner, J M]] | + | [[Category: Wagener R]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Werner JM]] |
| - | [[Category: Collagen vi 3n5]]
| + | |
| - | [[Category: Vwa]]
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| Structural highlights
Function
E9PWQ3_MOUSE
Publication Abstract from PubMed
Von Willebrand factor A (VWA) domains are versatile protein interaction domains with N and C termini in close proximity placing spatial constraints on overall protein structure. The 1.2 A crystal structures of a collagen VI VWA domain and a disease-causing point mutant show C-terminal extensions that place the N and C termini at opposite ends. This allows a "beads-on-a-string" arrangement of multiple VWA domains as observed for ten N-terminal domains of the collagen VI alpha3 chain. The extension is linked to the core domain by a salt bridge and two hydrophobic patches. Comparison of the wild-type and a muscular dystrophy-associated mutant structure identifies a potential perturbation of a protein interaction interface and indeed, the secretion of mutant collagen VI tetramers is affected. Homology modeling is used to locate a number of disease-associated mutations and analyze their structural impact, which will allow mechanistic analysis of collagen-VI-associated muscular dystrophy phenotypes.
A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein.,Becker AK, Mikolajek H, Paulsson M, Wagener R, Werner JM Structure. 2014 Feb 4;22(2):199-208. doi: 10.1016/j.str.2013.06.028. Epub 2013, Dec 12. PMID:24332716[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Becker AK, Mikolajek H, Paulsson M, Wagener R, Werner JM. A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein. Structure. 2014 Feb 4;22(2):199-208. doi: 10.1016/j.str.2013.06.028. Epub 2013, Dec 12. PMID:24332716 doi:http://dx.doi.org/10.1016/j.str.2013.06.028
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