Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster
Version of Record online: 22 NOV 2012
© 2012 The Authors Journal compilation © 2012 FEBS
The FEBS Journal
Volume 279, Issue 24, pages 4525–4534, December 2012
How to Cite
Akif, M., Masuyer, G., Bingham, R. J., Sturrock, E. D., Isaac, R. E. and Acharya, K. R. (2012), Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. The FEBS Journal, 279: 4525–4534. doi: 10.1111/febs.12038
- Issue online: 4 DEC 2012
- Version of Record online: 22 NOV 2012
- Accepted manuscript online: 20 OCT 2012 12:00AM EST
- Manuscript Accepted: 17 OCT 2012
- Manuscript Revised: 8 OCT 2012
- Manuscript Received: 6 AUG 2012
- Medical Research Council (UK). Grant Number: G1001685
- Wellcome Trust (UK). Grant Number: 088464
Fig. S1. The conversion of Ang I to Ang II (A, B) and the stability of Ang II (C, D) in the presence of recombinant AnCE.
Fig. S2. Sequential cleavage of Thr6–BK by AnCE.
Fig. S3. (A) Thr6–BK-bound AnCE crystal structure. AnCE (cyan), with Thr6–BK in magenta sticks. Citrate ion in grey. (B) Schematic view of Thr6–BK. Binding with hydrophobic interactions, hydrogen bonds and distances cited (grey).
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