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Cross-linking of mouse laminin 111

ABSTRACT: Laminin, a ~800 kD heterotrimeric protein, is a major functional component of the extracellular matrix, contributing to tissue development and maintenance. We used cross-linking and mass spectrometry to determine the order of subunits in the ~750 Å trimeric coiled-coil oligomerization domain of laminin and to achieve an estimate of the register of the three subunits along the length of the coiled coil.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Gad Armony

LAB HEAD: Deborah Fass

PROVIDER: PXD004898 | Pride | 2016-12-22

REPOSITORIES: Pride

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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]

PMID: 27815530

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Expression data from HT-1080 cells incubated or not in the presence of laminin111 coiled-coiled recombinant fragment (rLCC111)

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