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Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain.

Four individual LG modules from the C-terminus of the laminin alpha2 chain (LG1, LG2, LG4 and LG5) and combinations of these modules were prepared as recombinant products from transfected mammalian cells. This demonstrated that LG modules represent autonomously folding protein domains. Successful production depended on proper alignment of module borders and required a sequence correction at the C-terminus which added an extra cysteine. The LG modules were glycosylated and shown by electron microscopy to have a globular shape, indicating proper folding. Evidence is provided for the splicing of a 12 bp exon in LG2, although this did not impair folding. Proteolytic cleavage at the C-terminus of a basic sequence was observed close to the N-terminus of LG3. A similar processing also occurs in tissue-derived laminin-2 and -4 which contain the alpha2 chain.