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1hd9

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[[Image:1hd9.jpg|left|200px]]<br /><applet load="1hd9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hd9" />
 
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'''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF'''<br />
 
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==Overview==
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==The Bowman-Birk Inhibitor Reactive Site Loop Sequence Represents an Independent Structural Beta-Hairpin Motif==
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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.
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<StructureSection load='1hd9' size='340' side='right'caption='[[1hd9]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1HD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Known structural/functional Site: <scene name='pdbsite=P1:Primary Specificity Determinant For Inhib'>P1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1hd9" style="background-color:#fffaf0;"></div>
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[[Category: Brauer, A.B.E.]]
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== References ==
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[[Category: Cooke, R.M.]]
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<references/>
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[[Category: Kelly, G.]]
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__TOC__
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[[Category: Leatherbarrow, R.J.]]
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</StructureSection>
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[[Category: Matthews, S.J.]]
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[[Category: Large Structures]]
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[[Category: Mcbride, J.D.]]
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[[Category: Synthetic construct]]
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[[Category: bowman-birk inhibitor protein mimetic]]
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[[Category: Brauer ABE]]
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[[Category: human elastase inhibitor]]
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[[Category: Cooke RM]]
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[[Category: type vib beta-turn peptide]]
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[[Category: Kelly G]]
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[[Category: Leatherbarrow RJ]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:16:49 2007''
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[[Category: Matthews SJ]]
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[[Category: McBride JD]]

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The Bowman-Birk Inhibitor Reactive Site Loop Sequence Represents an Independent Structural Beta-Hairpin Motif

PDB ID 1hd9

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