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'''SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1''' | '''SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1''' | ||
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==About this Structure== | ==About this Structure== | ||
2BEY is a [[Single protein]] structure | 2BEY is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Leatherbarrow, R J.]] | [[Category: Leatherbarrow, R J.]] | ||
[[Category: Matthews, S J.]] | [[Category: Matthews, S J.]] | ||
[[Category: | [[Category: Bikk]] | ||
[[Category: | [[Category: C2 symmetrical bifunctional bicyclic trypsin inhibitor]] | ||
[[Category: | [[Category: Peptide]] | ||
[[Category: | [[Category: Sfti1]] | ||
[[Category: | [[Category: Symmetry]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:11:57 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:11, 3 May 2008
SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1
Overview
A novel bifunctional bicyclic inhibitor has been created that combines features both from the Bowman-Birk inhibitor (BBI) proteins, which have two distinct inhibitory sites, and from sunflower trypsin inhibitor-1 (SFTI-1), which has a compact bicyclic structure. The inhibitor was designed by fusing together a pair of reactive loops based on a sequence derived from SFTI-1 to create a backbone-cyclized disulfide-bridged 16-mer peptide. This peptide has two symmetrically spaced trypsin binding sites. Its synthesis and biological activity have been reported in a previous communication [Jaulent and Leatherbarrow, 2004, PEDS 17, 681]. In the present study we have examined the three-dimensional structure of the molecule. We find that the new inhibitor, which has a symmetrical 8-mer half-cystine CTKSIPP'I' motif repeated through a C2 symmetry axis also shows a complete symmetry in its three-dimensional structure. Each of the two loops adopts the expected canonical conformation common to all BBIs as well as SFTI-1. We also find that the inhibitor displays a strong and unique structural identity, with a notable lack of minor conformational isomers that characterise most reactive site loop mimics examined to date as well as SFTI-1. This suggests that the presence of the additional cyclic loop acts to restrict conformational mobility and that the deliberate introduction of cyclic symmetry may offer a general route to locking the conformation of beta-hairpin structures.
About this Structure
2BEY is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Solution structure of a novel C2-symmetrical bifunctional bicyclic inhibitor based on SFTI-1., Jaulent AM, Brauer AB, Matthews SJ, Leatherbarrow RJ, J Biomol NMR. 2005 Sep;33(1):57-62. PMID:16222558 Page seeded by OCA on Sat May 3 20:11:57 2008
