Nano-structure of the laminin γ-1 short arm reveals an extended and curved multidomain assembly

Trushar R. Patel, Gordon A. Morris, Daniela Zwolanek, Douglas R. Keene, Jianhua Li, Stephen E. Harding, Manuel Koch, Jörg Stetefeld

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Laminins are multidomain glycoproteins that play important roles in development and maintenance of the extracellular matrix via their numerous interactions with other proteins. Several receptors for the laminin short arms revealed their importance in network formation and intercellular signaling. However, both the detailed structure of the laminin γ-1 short arm and its organization within the complexes is poorly understood due to the complexity of the molecule and the lack of a high-resolution structure. The presented data provide the first subatomic resolution structure for the laminin γ-1 short arm in solution. This was achieved using an integrated approach that combined a number of complementary biophysical techniques such as small angle X-ray scattering (SAXS), analytical ultracentrifugation, dynamic light scattering and electron microscopy. As a result of this study, we have obtained a significantly improved model for the laminin γ-1 short arm that represents a major step forward in molecular understanding of laminin-mediated complex formations.

Original languageEnglish
Pages (from-to)565-572
Number of pages8
JournalMatrix Biology
Volume29
Issue number7
Early online date3 Aug 2010
DOIs
Publication statusPublished - Sep 2010
Externally publishedYes

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