Laminins bind Nidogens 1, 2
Species Homo sapiens
Nidogen-1 and nidogen-2, also known as the entactins, are basement membrane glycoproteins with three globular domains (G1, G2, G3) separated by rod-like regions. They form stable complexes with laminins and collagen IV (Fox et al. 1991, Talts et al. 1999, Salmivirta et al. 2002), thereby acting as a major linking agent between these two networks in basement membrane ECM (Nischt et al. 2007). Interactions mediated by HSPG2 (perlecan) (Behrens et al. 2012) or HSPG2 and agrin (Hohenester & Yurchenko 2013) have been proposed as an alternative basis for the association of the laminin and collagen type IV networks in basement membrane. Nidogen-1 binds to the laminin-1 gamma subunit (Mayer et al. 1998). The gamma-2 chain of laminin-332 contains a homologous binding module. Nidogen-1 was reportedly unable to bind this laminin (Mayer et al. 1995), though an N-terminal fragment was able to bind (Sasaki et al. 2001). Laminin gamma-3 has been shown to bind to nidogen-1 and -2 with a lower affinity than that of gamma-1 (Gersdorff et al. 2005). The ab initio reconstruction of complexes between nidogen-1 and the laminin gamma-1 short arm confirms that this interaction is mediated solely by the C-terminal domains (Patel et al. 2013).
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