Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies

被引:10
作者
Kulczyk, Arkadiusz W. [1 ]
McKee, Karen K. [2 ]
Zhang, Ximo [3 ]
Bizukojc, Iwona [3 ,4 ]
Yu, Ying Q. [3 ]
Yurchenco, Peter D. [2 ]
机构
[1] Rutgers State Univ, Inst Quantitat Biomed, Dept Biochem & Microbiol, Piscataway, NJ 08854 USA
[2] Rutgers State Univ, Robert Wood Johnson Med Sch, Dept Pathol & Lab Med, Piscataway, NJ 08854 USA
[3] Waters Corp, Milford, MA 01757 USA
[4] Cryo EMcorp, Bridgewater, NJ 08807 USA
关键词
NETWORK;
D O I
10.1038/s41467-023-36077-z
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 angstrom structure of the trimeric laminin polymer node containing alpha 1, beta 1 and gamma 1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. In this work the authors report the cryo-EM structure of the laminin polymer node and reveal the molecular basis of calcium-dependent formation of laminin lattice. The work provides insights into laminin polymerization defects manifesting in human disease.
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页数:7
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