2rel
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SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR, 11 STRUCTURES
OverviewOverview
The solution structure of r-elafin, a specific elastase inhibitor, has, been determined using NMR spectroscopy. Characterized by a flat core and a, flexible N-terminal extremity, the three-dimensional structure is formed, by a central twisted beta-hairpin accompanied by two external segments, linked by the proteinase binding loop. A cluster of three disulfide, bridges connects the external segments to the central beta-sheet and a, single fourth disulfide bridge links the binding loop to the central, beta-turn. The same spatial distribution of disulfide bridges can be, observed in both domains of the secretory leukocyte protease inhibitor, (SLPI), another elastase inhibitor. The structural homology between, r-elafin and the C-terminal domain of SLPI confirms the former as a second, member of the chelonianin family of proteinase inhibitors. Based on the, homology between the two proteins and recent results obtained for elastase, binding mutants of the bovine pancreatic trypsin inhibitor (BPTI), we, define the segment 22 to 27 as the binding loop of elafin, with the, scissile peptide bond between Ala24 and Met25. In our solution structures, this loop is extended and solvent-exposed, and exhibits a large degree of, flexibility. This mobility, already observed for the binding loop in other, protease inhibitors in solution, might be an important feature for the, interaction with the corresponding protease.
About this StructureAbout this Structure
2REL is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1REL. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of R-elafin, a specific inhibitor of elastase., Francart C, Dauchez M, Alix AJ, Lippens G, J Mol Biol. 1997 May 9;268(3):666-77. PMID:9171290
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