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{{Seed}}
[[Image:1hd9.png|left|200px]]


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==The Bowman-Birk Inhibitor Reactive Site Loop Sequence Represents an Independent Structural Beta-Hairpin Motif==
The line below this paragraph, containing "STRUCTURE_1hd9", creates the "Structure Box" on the page.
<StructureSection load='1hd9' size='340' side='right'caption='[[1hd9]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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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>
{{STRUCTURE_1hd9|  PDB=1hd9  |  SCENE=  }}
<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.


===THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_11243789}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11243789 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11243789}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1HD9 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA].
[[Category: Synthetic construct]]
 
[[Category: Brauer ABE]]
==Reference==
[[Category: Cooke RM]]
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://www.ncbi.nlm.nih.gov/pubmed/11243789 11243789]
[[Category: Kelly G]]
[[Category: Single protein]]
[[Category: Leatherbarrow RJ]]
[[Category: Brauer, A B.E.]]
[[Category: Matthews SJ]]
[[Category: Cooke, R M.]]
[[Category: McBride JD]]
[[Category: Kelly, G.]]
[[Category: Leatherbarrow, R J.]]
[[Category: Matthews, S J.]]
[[Category: Mcbride, J D.]]
[[Category: Bowman-birk inhibitor protein mimetic]]
[[Category: Human elastase inhibitor]]
[[Category: Type vib beta-turn peptide]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:01:23 2008''

Latest revision as of 00:02, 21 November 2024

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

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