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PDBsum entry 2rel
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Serine protease inhibitor
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PDB id
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2rel
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References listed in PDB file
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Key reference
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Title
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Solution structure of r-Elafin, A specific inhibitor of elastase.
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Authors
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C.Francart,
M.Dauchez,
A.J.Alix,
G.Lippens.
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Ref.
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J Mol Biol, 1997,
268,
666-677.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 4.
Figure 4. HSQC spectrum of r-elafin in
2
H2O at pH 7
and at 293 K showing most of the
13
C
a
resonances, all
proline
13
C
d
resonances (Pd) and the three serine
13
C
b
resonances (Sb).
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Figure 6.
Figure 6. A representation of the different inter-proton
NOEs ( !) and the strong hydrogen bonds ( ) in
the b-sheet.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1997,
268,
666-677)
copyright 1997.
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Secondary reference #1
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Title
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Synthesis and structure-Activity relationships of elafin, An elastase-Specific inhibitor.
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Authors
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M.Tsunemi,
H.Kato,
Y.Nishiuchi,
S.Kumagaye,
S.Sakakibara.
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Ref.
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Biochem Biophys Res Commun, 1992,
185,
967-973.
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PubMed id
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Secondary reference #2
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Title
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Erratum. Elafin: an elastase-Specific inhibitor of human skin. Purification, Characterization, And complete amino acid sequence
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Authors
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O.Wiedow,
J.M.Schroder,
H.Gregory,
J.A.Young,
E.Christophers.
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Ref.
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j biol chem, 1991,
266,
3356.
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Secondary reference #3
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Title
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Elafin: an elastase-Specific inhibitor of human skin. Purification, Characterization, And complete amino acid sequence.
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Authors
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O.Wiedow,
J.M.Schröder,
H.Gregory,
J.A.Young,
E.Christophers.
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Ref.
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J Biol Chem, 1990,
265,
14791-14795.
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PubMed id
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