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Matrix Biol. 2010 Sep;29(7):565-72. doi: 10.1016/j.matbio.2010.07.004. Epub 2010 Aug 3.

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

Author information

1
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2.

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.

PMID:
20688161
DOI:
10.1016/j.matbio.2010.07.004
[Indexed for MEDLINE]

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