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| [[Image:1hd9.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1hd9| PDB=1hd9 | SCENE= }} | | {{STRUCTURE_1hd9| PDB=1hd9 | SCENE= }} |
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| '''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=== |
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| ==Overview==
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11243789}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11243789 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11243789}} |
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| ==About this Structure== | | ==About this Structure== |
| 1HD9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA]. | | 1HD9 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Human elastase inhibitor]] | | [[Category: Human elastase inhibitor]] |
| [[Category: Type vib beta-turn peptide]] | | [[Category: Type vib beta-turn peptide]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:43:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:01:23 2008'' |
