|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==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== |
| - | <StructureSection load='1hd9' size='340' side='right'caption='[[1hd9]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1hd9' size='340' side='right'caption='[[1hd9]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hd9]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HD9 FirstGlance]. <br> | + | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr> | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hd9 OCA], [http://pdbe.org/1hd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hd9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hd9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hd9 ProSAT]</span></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> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 21: |
Line 22: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brauer, A B.E]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Cooke, R M]] | + | [[Category: Brauer ABE]] |
| - | [[Category: Kelly, G]] | + | [[Category: Cooke RM]] |
| - | [[Category: Leatherbarrow, R J]] | + | [[Category: Kelly G]] |
| - | [[Category: Matthews, S J]] | + | [[Category: Leatherbarrow RJ]] |
| - | [[Category: McBride, J D]] | + | [[Category: Matthews SJ]] |
| - | [[Category: Bowman-birk inhibitor protein mimetic]]
| + | [[Category: McBride JD]] |
| - | [[Category: Human elastase inhibitor]]
| + | |
| - | [[Category: Hydrolase inhibitor]]
| + | |
| - | [[Category: Peptide inhibitor]]
| + | |
| - | [[Category: Type vib beta-turn peptide]]
| + | |
| Structural highlights
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.,Brauer AB, Kelly G, McBride JD, Cooke RM, Matthews SJ, Leatherbarrow RJ J Mol Biol. 2001 Mar 2;306(4):799-807. PMID:11243789[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brauer AB, Kelly G, McBride JD, Cooke RM, Matthews SJ, Leatherbarrow RJ. The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural beta-hairpin motif. J Mol Biol. 2001 Mar 2;306(4):799-807. PMID:11243789 doi:10.1006/jmbi.2000.4410
|
