Figure 1.

Schematic organization of human type VII collagen and cDNA constructs generated for this study for expressing recombinant peptides of the NC1 domain. Type VII collagen is composed of 3 identical α chains, each consisting of a central triple helical collagenous domain, flanked by a large amino-terminal noncollagenous domain (NC1) and a smaller carboxy-terminal noncollagenous domain (NC2). Two molecules form antiparallel tail-to-tail dimers stabilized by disulfide bonding through a carboxy-terminal overlap between NC2 domains. Three fragments of murine type VII collagen cDNA were cloned in pGEX-6P-1 and expressed in E. coli. Amino acid residue numbers are shown below the fragments.