1hd9
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(New page: 200px<br /> <applet load="1hd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hd9" /> '''THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOO...)
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Revision as of 19:23, 29 October 2007
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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, ... [(full description)]
About this Structure
1HD9 is a [Single protein] structure of sequence from [[1]]. 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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