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

Patel, T. R., Morris, Gordon, Zwolanek, D., Keene, D. R., Li, J., Harding, S. E., Koch, M. and Stetefeld, J. (2010) Nano-structure of the laminin gamma-1 short arm reveals an extended and curved multidomain assembly. Matrix Biology, 29 (7). pp. 565-572. ISSN 0945-053X

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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 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. © 2010.

Item Type: Article
Uncontrolled Keywords: Ab initio modeling Analytical ultracentrifugation Dynamic light scattering Laminin Rotary shadowing Small angle X-ray scattering laminin gamma1 nanomaterial article electron microscopy light scattering molecular dynamics priority journal protein structure signal transduction ultracentrifugation X ray crystallography
Subjects: Q Science > QD Chemistry
Schools: School of Applied Sciences
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Depositing User: Gordon Morris
Date Deposited: 18 May 2011 11:57
Last Modified: 28 Aug 2021 11:06


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