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. 2011 Feb 25;3(1):883–896. doi: 10.3390/cancers3010883

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© 2011 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 2. — Structures of the non-processed laminin-332 and laminin-511. A characteristic hallmark of laminins is the α-helical coiled-coil domain consisting of three laminin chains, α3β3γ2 or α5β1γ1 for laminin-332 and laminin-511, respectively. Each chain can be cleaved by several different proteases with drastic effects on its biological functions. Exclusively formed by the C-terminal portion of the α3 chain, the globular (G) domain can be subdivided into five LG-domains, each about 200 amino acids in length. The LG4-5 tandem domain is connected to the LG1-3 domain cluster via connecting sequence. The connecting sequence contains target sites for several proteases. The G-domain contains the putative binding site for the integrins α3β1, α6β1, and α6β4. Secreted laminin-332 undergoes fast processing by proteases which cleave the LG4-5 domain of the α3 chain and the N-terminal domain of the γ2 chain.