Structural elucidation of full-length nidogen and the laminin-nidogen complex in solution

Patel, Trushar R., Bernards, Claudia, Meier, Markus, McEleney, Kevin, Winzor, Donald J., Koch, Manuel and Stetefeld, Jorg (2014) Structural elucidation of full-length nidogen and the laminin-nidogen complex in solution. Matrix Biology, 33 60-67. doi:10.1016/j.matbio.2013.07.009

Author Patel, Trushar R.
Bernards, Claudia
Meier, Markus
McEleney, Kevin
Winzor, Donald J.
Koch, Manuel
Stetefeld, Jorg
Title Structural elucidation of full-length nidogen and the laminin-nidogen complex in solution
Journal name Matrix Biology   Check publisher's open access policy
ISSN 0945-053X
Publication date 2014-01
Year available 2013
Sub-type Article (original research)
DOI 10.1016/j.matbio.2013.07.009
Open Access Status
Volume 33
Start page 60
End page 67
Total pages 8
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Collection year 2014
Language eng
Formatted abstract
Nidogen-1 is a key basement membrane protein that is required for many biological activities. It is one of the central elements in organizing basal laminae including those in the skin, muscle, and the nervous system. The self-assembling extracellular matrix that also incorporates fibulins, fibronectin and integrins is clamped together by networks formed between nidogen, perlecan, laminin and collagen IV. To date, the full-length version of nidogen-1 has not been studied in detail in terms of its solution conformation and shape because of its susceptibility to proteolysis. In the current study, we have expressed and purified full-length nidogen-1 and have investigated its solution behavior using size-exclusion chromatography (SEC), dynamic light scattering (DLS) and small angle X-ray scattering (SAXS). The ab initio shape reconstruction of the complex between nidogen-1 and the laminin γ-1 short arm confirms that the interaction is mediated solely by the C-terminal domains: the rest of the domains of both proteins do not participate in complex formation.
Keyword Dynamic light scattering
Extracellular matrix proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 5 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 5 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 11 Mar 2014, 01:27:37 EST by System User on behalf of School of Chemistry & Molecular Biosciences