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Title | Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 317, Year 2023 |
Publish date | Jan 19, 2023 |
Authors | Arkadiusz W Kulczyk / Karen K McKee / Ximo Zhang / Iwona Bizukojc / Ying Q Yu / Peter D Yurchenco / |
PubMed Abstract | 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 ...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 Å structure of the trimeric laminin polymer node containing α1, β1 and γ1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. |
External links | Nat Commun / PubMed:36658135 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 Å |
Structure data | EMDB-27542, PDB-8dmk: |
Chemicals | ChemComp-NAG: ChemComp-CA: |
Source |
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Keywords | STRUCTURAL PROTEIN / Laminin / Complex / Basement membrane |