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Cross-linking reveals laminin coiled-coil architecture.


ABSTRACT: Laminin, an ?800-kDa heterotrimeric protein, is a major functional component of the extracellular matrix, contributing to tissue development and maintenance. The unique architecture of laminin is not currently amenable to determination at high resolution, as its flexible and narrow segments complicate both crystallization and single-particle reconstruction by electron microscopy. Therefore, we used cross-linking and MS, evaluated using computational methods, to address key questions regarding laminin quaternary structure. This approach was particularly well suited to the ?750-Å coiled coil that mediates trimer assembly, and our results support revision of the subunit order typically presented in laminin schematics. Furthermore, information on the subunit register in the coiled coil and cross-links to downstream domains provide insights into the self-assembly required for interaction with other extracellular matrix and cell surface proteins.

SUBMITTER: Armony G 

PROVIDER: S-EPMC5127338 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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Cross-linking reveals laminin coiled-coil architecture.

Armony Gad G   Jacob Etai E   Moran Toot T   Levin Yishai Y   Mehlman Tevie T   Levy Yaakov Y   Fass Deborah D  

Proceedings of the National Academy of Sciences of the United States of America 20161104 47


Laminin, an ∼800-kDa heterotrimeric protein, is a major functional component of the extracellular matrix, contributing to tissue development and maintenance. The unique architecture of laminin is not currently amenable to determination at high resolution, as its flexible and narrow segments complicate both crystallization and single-particle reconstruction by electron microscopy. Therefore, we used cross-linking and MS, evaluated using computational methods, to address key questions regarding la  ...[more]

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