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New page: left|200px<br /> <applet load="1hd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hd9" /> '''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOO...
 
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[[Image:1hd9.gif|left|200px]]<br />
<applet load="1hd9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hd9" />
'''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF'''<br />


==Overview==
==The Bowman-Birk Inhibitor Reactive Site Loop Sequence Represents an Independent Structural Beta-Hairpin Motif==
We have determined the NMR structure in aqueous solution of a, disulphide-cyclised 11-residue peptide that forms a stable beta-hairpin, incorporating a type VIb beta-turn. The structure is found to be extremely, well ordered for a short peptide, with the 30 lowest energy simulated, annealing structures having an average pairwise r.m.s. deviation of only, 0.36 A over the backbone. All but three side-chains adopt distinct, conformations, allowing a detailed analysis of their involvement in, cross-strand interactions. The peptide sequence analysed originates from a, previously reported study, which identified potent inhibitors of human, leukocyte elastase from screening a combinatorial peptide library based on, the short protein beta-sheet segment that forms the reactive site loop of, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11243789 (full description)]]
<StructureSection load='1hd9' size='340' side='right'caption='[[1hd9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hd9]] 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=1HD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HD9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></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=1hd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hd9 OCA], [https://pdbe.org/1hd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hd9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hd9 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the NMR structure in aqueous solution of a disulphide-cyclised 11-residue peptide that forms a stable beta-hairpin, incorporating a type VIb beta-turn. The structure is found to be extremely well ordered for a short peptide, with the 30 lowest energy simulated annealing structures having an average pairwise r.m.s. deviation of only 0.36 A over the backbone. All but three side-chains adopt distinct conformations, allowing a detailed analysis of their involvement in cross-strand interactions. The peptide sequence analysed originates from a previously reported study, which identified potent inhibitors of human leukocyte elastase from screening a combinatorial peptide library based on the short protein beta-sheet segment that forms the reactive site loop of Bowman-Birk inhibitors. A detailed comparison of the peptide's solution structure with the corresponding region in the whole protein structure reveals a very good correspondence not only for the backbone (r.m.s. deviation approximately 0.7 A) but also for the side-chains. This isolated beta-hairpin retains the biologically active "canonical conformation" typical of small serine proteinase inhibitor proteins, which explains why it retains inhibitory activity. Since the structural integrity is sequence-inherent and does not depend upon the presence of the remaining protein, this beta-hairpin represents an independent structural motif and so provides a useful model of this type of protein architecture and its relation to biological function. The relationship between the conformation of this beta-hairpin and its biological activity is discussed.


==About this Structure==
The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural beta-hairpin motif.,Brauer AB, Kelly G, McBride JD, Cooke RM, Matthews SJ, Leatherbarrow RJ J Mol Biol. 2001 Mar 2;306(4):799-807. PMID:11243789<ref>PMID:11243789</ref>
1HD9 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural beta-hairpin motif., Brauer AB, Kelly G, McBride JD, Cooke RM, Matthews SJ, Leatherbarrow RJ, J Mol Biol. 2001 Mar 2;306(4):799-807. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11243789 11243789]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1hd9" style="background-color:#fffaf0;"></div>
[[Category: Brauer, A.B.E.]]
== References ==
[[Category: Cooke, R.M.]]
<references/>
[[Category: Kelly, G.]]
__TOC__
[[Category: Leatherbarrow, R.J.]]
</StructureSection>
[[Category: Matthews, S.J.]]
[[Category: Large Structures]]
[[Category: Mcbride, J.D.]]
[[Category: Synthetic construct]]
[[Category: bowman-birk inhibitor protein mimetic]]
[[Category: Brauer ABE]]
[[Category: human elastase inhibitor]]
[[Category: Cooke RM]]
[[Category: type vib beta-turn peptide]]
[[Category: Kelly G]]
 
[[Category: Leatherbarrow RJ]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:27:56 2007''
[[Category: Matthews SJ]]
[[Category: McBride JD]]
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