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TitleCryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 317, Year 2023
Publish dateJan 19, 2023
AuthorsArkadiusz W Kulczyk / Karen K McKee / Ximo Zhang / Iwona Bizukojc / Ying Q Yu / Peter D Yurchenco /
PubMed AbstractLaminin 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 linksNat Commun / PubMed:36658135 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

27542

8dmk

EMDB-27542, PDB-8dmk:
Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN / Laminin / Complex / Basement membrane

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