Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin
Article first published online: 12 NOV 2012
© 2012 The Authors Journal compilation © 2012 FEBS
Volume 279, Issue 24, pages 4466–4478, December 2012
How to Cite
Derache, C., Epinette, C., Roussel, A., Gabant, G., Cadene, M., Korkmaz, B., Gauthier, F. and Kellenberger, C. (2012), Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin. FEBS Journal, 279: 4466–4478. doi: 10.1111/febs.12033
- Issue published online: 4 DEC 2012
- Article first published online: 12 NOV 2012
- Accepted manuscript online: 17 OCT 2012 12:00AM EST
- Manuscript Accepted: 9 OCT 2012
- Manuscript Revised: 5 OCT 2012
- Manuscript Received: 29 AUG 2012
- Region Centre and the Fonds Européen de Développement Régional
- Fonds Européen de Développement Régional. Grant Number: #2699-33931
Fig. S1. Ultra-high-resolution QTOF CID fragmentation of dephosphorylated greglin (1–27).
Fig. S2. Ultra-high-resolution QTOF CID fragmentation of greglin (28–51).
Fig. S3. Pseudo-MS3 ultra-high-resolution QTOF fragmentation of dephosphorylated greglin (1–27).
Fig. S4. MALDI-TOF MS of immobilized metal-affinity chromatography-enriched tryptic greglin phosphopeptides.
Fig. S5. UHR-QTOF CID fragmentation of mono-phosphorylated [1-27]* greglin peptide.
Fig. S6. Hydrogen bonds between the RSL of greglin and subtilisin.
Fig. S7. Superposition of greglin with canonical inhibitors from various families.
Fig. S8. Superposition of the RSLs of greglin with those of OMTKY3 in complex with subtilisin, chymotrypsin and human neutrophil elastase.
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