1hd9
From Proteopedia
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| - | [[Image:1hd9.jpg|left|200px]]<br /><applet load="1hd9" size=" | + | [[Image:1hd9.jpg|left|200px]]<br /><applet load="1hd9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hd9" /> | caption="1hd9" /> | ||
'''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF'''<br /> | '''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1HD9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: type vib beta-turn peptide]] | [[Category: type vib beta-turn peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:48:38 2008'' |
Revision as of 07:48, 3 February 2008
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THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP SEQUENCE REPRESENTS AN INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF
Overview
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
1HD9 is a Single protein structure of sequence from [1]. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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