2bey
From Proteopedia
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| - | [[Image:2bey.gif|left|200px]] | + | [[Image:2bey.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1''' | + | {{Structure |
| + | |PDB= 2bey |SIZE=350|CAPTION= <scene name='initialview01'>2bey</scene> | ||
| + | |SITE= <scene name='pdbsite=P1A:Specificity+Determinant+For+Inhibition+Site_identifier+P1b'>P1A</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BEY is a [ | + | 2BEY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16222558 16222558] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brauer, A B.E.]] | [[Category: Brauer, A B.E.]] | ||
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[[Category: symmetry]] | [[Category: symmetry]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:06 2008'' |
Revision as of 14:01, 20 March 2008
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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 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 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 Thu Mar 20 16:01:06 2008
