2bey: Difference between revisions
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New page: left|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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== | ==Solution Structure of a Novel C2 Symmetrical Bifunctional Bicyclic Inhibitor Based on SFTI-1== | ||
A novel bifunctional bicyclic inhibitor has been created that combines | <StructureSection load='2bey' size='340' side='right'caption='[[2bey]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bey]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BEY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bey OCA], [https://pdbe.org/2bey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bey RCSB], [https://www.ebi.ac.uk/pdbsum/2bey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bey ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:16222558</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bey" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Brauer ABE]] | ||
[[Category: | [[Category: Jaulent AM]] | ||
[[Category: Leatherbarrow RJ]] | |||
[[Category: Matthews SJ]] | |||
