27.11
Type IV collagens are non-fibrillar or network-forming collagens which are primarily found in the basal lamina.
A typical type IV collagen is a 400 nm long, triple-helical structure interrupted by several non-helical regions which add flexibility to the molecule.
At the N-terminal, it has a small globular domain, while a large globular domain is present at the C-terminal.
Through these terminal globular domains, the collagen fibres can associate with each other by head-to-head interactions forming a dimer; and tail-to-tail interactions forming a tetramer. The fibres also associate by lateral interactions between the triple-helical regions.
Such complex associations can form a two dimensional, irregular network, which provides tensile strength to the basal lamina.
This network further links with the laminin lattice and other glycoproteins such as perlecan and entactin, to build a complete basal lamina.
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen form…
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