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Triple helical organization of the type IV collagen family

Triple helical organization of the type IV collagen family
Six genetically distinct alpha chains are arranged into three triple helical protomers that differ in their chain composition. Each protomer has an 7S triple helical domain at the N-terminal; a long, triple helical, collagenous domain in the middle of the molecule; and an NC1 trimer at the C-terminal. Interruptions in the Gly–Xaa–Yaa amino acid sequence at multiple sites along the collagenous domain (white rings) confer flexibility, allowing for looping and supercoiling of protomers into networks. The selection of chains for association into trimeric protomers is governed by molecular recognition sequences encoded within the hypervariable regions of NC1 domains.[1,2]
NC1: noncollagenous.
References:
  1. Boutaud A, Borza DB, Bondar O, et al. Type IV collagen of the glomerular basement membrane: Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains. J Biol Chem 2000; 275:30716.
  2. Borza DB, Bondar O, Ninomiya Y, et al. The NC1 domain of collagen IV encodes a novel network composed of the alpha 1, alpha 2, alpha 5, and alpha 6 chains in smooth muscle basement membranes. J Biol Chem 2001; 276:28532.

From: Hudson BG, Tryggvason K, Sundaramoorthy M, Neilson EG. Alport's syndrome, Goodpasture's syndrome, and type IV collagen. N Engl J Med 2003; 348:2543. Copyright © 2003 Massachusetts Medical Society. Reprinted with permission from Massachusetts Medical Society.

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