The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
Coates, L., Erskine, P.T., Mall, S., Williams, P.A., Gill, R.S., Wood, S.P. and Cooper, J.B. (2003) The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom. Acta Crystallographica Section D, Biological Crystallography, 59, (6), 978-981. (doi:10.1107/S0907444903006267).
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Description/Abstract
The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 Å. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.
| Item Type: | Article |
|---|---|
| ISSNs: | 0907-4449 (print) |
| Related URLs: | |
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Divisions: | University Structure - Pre August 2011 > School of Biological Sciences |
| Item ID: | 56799 |
| Date Deposited: | 06 Aug 2008 |
| Last Modified: | 12 May 2013 01:19 |
| Contributors: | Coates, L. (Author) Erskine, P.T. (Author) Mall, S. (Author) Williams, P.A. (Author) Gill, R.S. (Author) Wood, S.P. (Author) Cooper, J.B. (Author) |
| Date: | 1 June 2003 |
| Status: | Published |
| URI: | http://eprints.soton.ac.uk/id/eprint/56799 |
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