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| - | [[Image:2bey.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bey| PDB=2bey | SCENE= }} | | {{STRUCTURE_2bey| PDB=2bey | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16222558}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16222558 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16222558}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2BEY is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEY OCA]. | + | 2BEY is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEY OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Sfti1]] | | [[Category: Sfti1]] |
| | [[Category: Symmetry]] | | [[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 Tue Jul 29 15:00:05 2008'' |
Revision as of 12:00, 29 July 2008
Template:STRUCTURE 2bey
SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1
Template:ABSTRACT PUBMED 16222558
About this Structure
2BEY is a Single protein structure. Full experimental 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 Tue Jul 29 15:00:05 2008
