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Matrix Biol. 2014 Jan;33:60-7. doi: 10.1016/j.matbio.2013.07.009. Epub 2013 Aug 12.

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

Author information

1
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada.
2
Institute for Dental Research and Oral Musculoskeletal Biology, Center for Molecular Medicine Cologne, Center for Biochemistry, Medical Faculty, University of Cologne, D-50931 Cologne, Germany.
3
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland, 4072, Australia.
4
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada; Microbiology, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada; Biochemistry and Medical Genetics, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada. Electronic address: jorg.stetefeld@ad.manitoba.ca.

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.

KEYWORDS:

Dynamic light scattering; Extracellular matrix proteins; Hydrodynamics; Laminin; Nidogen-1; Small angle X-ray scattering

PMID:
23948589
DOI:
10.1016/j.matbio.2013.07.009
[Indexed for MEDLINE]
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