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.

authors

Armony G,Jacob E,Moran T,Levin Y,Mehlman T,Levy Y,Fass D

doi

10.1073/pnas.1608424113

subject

Has Abstract

pub_date

2016-11-22 00:00:00

pages

13384-13389

issue

47

eissn

0027-8424

issn

1091-6490

pii

1608424113

journal_volume

113

pub_type

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