Abstract
Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and 1H, 15N, 13C chemical shift assignment of a subdomain of the murine type VII collagen - the von-Willebrand-factor-A-like domain 2 (mvWFA2). vWFA2 interacts with type I collagen and plays a central role in certain skin blistering diseases. Based on these assignments a secondary structure prediction was performed showing a properly folded protein. An interaction of mvWFA2 with its neighboring domain mFNIII-9 was characterized with NMR spectroscopy and SPR.
| Original language | English |
|---|---|
| Journal | FEBS Letters |
| Volume | 585 |
| Issue number | 12 |
| Pages (from-to) | 1748-1752 |
| Number of pages | 5 |
| ISSN | 0014-5793 |
| DOIs | |
| Publication status | Published - 23.06.2011 |
Funding
This work was supported by the cluster of excellence “inflammation at interfaces” of the DFG (EXC 306/1). The authors thank J. Brümmer for the BIAcore measurements and T. Peters and R. Ludwig for critical reading of the manuscript. The eNMR project (European FP7 e-Infrastructure grant, contract no. 213010, www.enmr.eu ), supported by the national GRID Initiatives of Italy, Germany and the Dutch BiG Grid project (Netherlands Organization for Scientific Research), is acknowledged for the use of web portals, computing and storage facilities. Chemical shift data has been deposited in BioMagResBank under the accession number 17549 (http://www.bmrb.wisc.edu/). Appendix A
