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2bey
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(New page: 200px<br /> <applet load="2bey" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bey" /> '''SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICA...)
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Revision as of 18:52, 29 October 2007
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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, ... [(full description)]
About this Structure
2BEY is a [Single protein] structure of sequence from [[1]]. 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 Mon Oct 29 20:57:28 2007
