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8dmk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies== | |
| + | <StructureSection load='8dmk' size='340' side='right'caption='[[8dmk]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8dmk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DMK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8dmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dmk OCA], [https://pdbe.org/8dmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dmk RCSB], [https://www.ebi.ac.uk/pdbsum/8dmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dmk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LAMA1_MOUSE LAMA1_MOUSE] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron microscopy to determine a 3.7 A structure of the trimeric laminin polymer node containing alpha1, beta1 and gamma1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. | ||
| - | + | Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies.,Kulczyk AW, McKee KK, Zhang X, Bizukojc I, Yu YQ, Yurchenco PD Nat Commun. 2023 Jan 19;14(1):317. doi: 10.1038/s41467-023-36077-z. PMID:36658135<ref>PMID:36658135</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8dmk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Kulczyk AW]] | ||
Revision as of 11:21, 1 February 2023
Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies
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