The solution structure of the kallikrein-related peptidases inhibitor SPINK6

Sascha Jung, Jan Fischer, Björn Spudy, Tim Kerkow, Frank D. Sönnichsen, Li Xue, Alexandre M.J.J. Bonvin, Peter Goettig, Viktor Magdolen, Ulf Meyer-Hoffert, Joachim Grötzinger

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Kallikrein-related peptidases (KLKs) are crucial for epidermal barrier function and are involved in the proteolytic regulation of the desquamation process. Elevated KLK levels were reported in atopic dermatitis. In skin, the proteolytic activity of KLKs is regulated by specific inhibitors of the serine protease inhibitor of Kazal-type (SPINK) family. SPINK6 was shown to be expressed in human stratum corneum and is able to inhibit several KLKs such as KLK4, -5, -12, -13 and -14. In order to understand the structural traits of the specific inhibition we solved the structure of SPINK6 in solution by NMR-spectroscopy and studied its interaction with KLKs. Thereby, beside the conserved binding mode, we identified an alternate binding mode which has so far not been observed for SPINK inhibitors.

Original languageEnglish
Pages (from-to)103-108
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 26 Feb 2016
Externally publishedYes


  • KLK4
  • Kallikrein-related peptidase 4
  • Model protease - inhibitor complex
  • Nuclear magnetic resonance
  • SPINK6
  • Structure


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