The NC16A domain of collagen XVII plays a role in triple helix assembly and stability.
Collagen XVII/BP180 is a transmembrane constituent of the epidermal anchoring complex. To study the role of its non-collagenous linker domain, NC16A, in protein assembly and stability, we analyzed the following recombinant proteins: the collagen XVII extracellular domain with or without NC16A, and a pair of truncated proteins comprising the COL15-NC15 stretch expressed with or without NC16A. All four proteins were found to exist as stable collagen triple helices; however, the two missing NC16A exhibited melting temperatures significantly lower than their NC16A-containing counterparts. Protein refolding experiments revealed that the rate of triple helix assembly of the collagen model peptide GPP(10) is greatly increased by the addition of an upstream NC16A domain. In summary, the NC16A linker domain of collagen XVII exhibits a positive effect on both the rate of assembly and the stability of the adjoining collagen structure.
Van den Bergh
Françoise
F
Department of Dermatology, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA. fvdbergh@mcw.edu
Fu
Chang-Ling
CL
Olague-Marchan
Monica
M
Giudice
George J
GJ
D001324:Autoantigens / Q000737:chemistry*; D001665:Binding Sites; D024041:Non-Fibrillar Collagens / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D000097805:Collagen Type XVII
D001324:Autoantigens; D024041:Non-Fibrillar Collagens; D000097805:Collagen Type XVII