1hd9
From Proteopedia
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|PDB= 1hd9 |SIZE=350|CAPTION= <scene name='initialview01'>1hd9</scene> | |PDB= 1hd9 |SIZE=350|CAPTION= <scene name='initialview01'>1hd9</scene> | ||
|SITE= <scene name='pdbsite=P1:Primary+Specificity+Determinant+For+Inhib'>P1</scene> | |SITE= <scene name='pdbsite=P1:Primary+Specificity+Determinant+For+Inhib'>P1</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1hd9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hd9 RCSB]</span> | ||
}} | }} | ||
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[[Category: type vib beta-turn peptide]] | [[Category: type vib beta-turn peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:44 2008'' |
Revision as of 18:02, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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