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| | ==IgM C4-domain from mouse== | | ==IgM C4-domain from mouse== |
| - | <StructureSection load='4jvw' size='340' side='right' caption='[[4jvw]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4jvw' size='340' side='right'caption='[[4jvw]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jvw]] is a 4 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=4JVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JVW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jvw]] is a 4 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=4JVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JVW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jvu|4jvu]]</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=4jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jvw OCA], [https://pdbe.org/4jvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jvw RCSB], [https://www.ebi.ac.uk/pdbsum/4jvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jvw ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Igh-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jvw OCA], [http://pdbe.org/4jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jvw RCSB], [http://www.ebi.ac.uk/pdbsum/4jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jvw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/IGHM_MOUSE IGHM_MOUSE] |
| | <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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Buchner, J]] | + | [[Category: Mus musculus]] |
| - | [[Category: Graewert, A M]] | + | [[Category: Buchner J]] |
| - | [[Category: Groll, M]] | + | [[Category: Graewert AM]] |
| - | [[Category: Kern, T]] | + | [[Category: Groll M]] |
| - | [[Category: Madl, T]] | + | [[Category: Kern T]] |
| - | [[Category: Mueller, R]] | + | [[Category: Madl T]] |
| - | [[Category: Peschek, J]] | + | [[Category: Mueller R]] |
| - | [[Category: Sattler, M]] | + | [[Category: Peschek J]] |
| - | [[Category: Antibody]]
| + | [[Category: Sattler M]] |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Immunoglobulin m]]
| + | |
| - | [[Category: Oligomerization]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
Function
IGHM_MOUSE
Publication Abstract from PubMed
IgM is the first antibody produced during the humoral immune response. Despite its fundamental role in the immune system, IgM is structurally only poorly described. In this work we used X-ray crystallography and NMR spectroscopy to determine the atomic structures of the constant IgM Fc domains (Cmicro2, Cmicro3, and Cmicro4) and to address their roles in IgM oligomerization. Although the isolated domains share the typical Ig fold, they differ substantially in dimerization properties and quaternary contacts. Unexpectedly, the Cmicro4 domain and its C-terminal tail piece are responsible and sufficient for the specific polymerization of Cmicro4 dimers into covalently linked hexamers of dimers. Based on small angle X-ray scattering data, we present a model of the ring-shaped Cmicro4 structure, which reveals the principles of IgM oligomerization.
High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation.,Muller R, Grawert MA, Kern T, Madl T, Peschek J, Sattler M, Groll M, Buchner J Proc Natl Acad Sci U S A. 2013 Jun 18;110(25):10183-8. doi:, 10.1073/pnas.1300547110. Epub 2013 Jun 3. PMID:23733956[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muller R, Grawert MA, Kern T, Madl T, Peschek J, Sattler M, Groll M, Buchner J. High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation. Proc Natl Acad Sci U S A. 2013 Jun 18;110(25):10183-8. doi:, 10.1073/pnas.1300547110. Epub 2013 Jun 3. PMID:23733956 doi:10.1073/pnas.1300547110
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