2N52
The solution structure of the kallikrein inhibitor SPINK6
Summary for 2N52
| Entry DOI | 10.2210/pdb2n52/pdb |
| NMR Information | BMRB: 25691 |
| Descriptor | Serine protease inhibitor Kazal-type 6 (1 entity in total) |
| Functional Keywords | inhibitor, hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted : Q6UWN8 |
| Total number of polymer chains | 1 |
| Total formula weight | 6411.24 |
| Authors | Grotzinger, J. (deposition date: 2015-07-06, release date: 2016-03-16, Last modification date: 2024-11-06) |
| Primary citation | Jung, S.,Fischer, J.,Spudy, B.,Kerkow, T.,Sonnichsen, F.D.,Xue, L.,Bonvin, A.M.,Goettig, P.,Magdolen, V.,Meyer-Hoffert, U.,Grotzinger, J. The solution structure of the kallikrein-related peptidases inhibitor SPINK6. Biochem.Biophys.Res.Commun., 471:103-108, 2016 Cited by PubMed Abstract: 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. PubMed: 26828269DOI: 10.1016/j.bbrc.2016.01.172 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
