4.6 Article

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

Journal

MATRIX BIOLOGY
Volume 29, Issue 7, Pages 565-572

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2010.07.004

Keywords

Laminin; Small angle X-ray scattering; Ab initio modeling; Analytical ultracentrifugation; Dynamic light scattering; Rotary shadowing

Funding

  1. Manitoba Health Research Council/Manitoba Institute of Child Health
  2. CIHR
  3. Province of Manitoba

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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 gamma-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 gamma-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 gamma-1 short arm that represents a major step forward in molecular understanding of laminin-mediated complex formations. Crown Copyright (C) 2010 Published by Elsevier B.V. All rights reserved.

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