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PDBsum entry 1bma
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Hydrolase/hydrolase inhibitor
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PDB id
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1bma
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Interaction of a peptidomimetic aminimide inhibitor with elastase.
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Authors
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E.Peisach,
D.Casebier,
S.L.Gallion,
P.Furth,
G.A.Petsko,
J.C.Hogan,
D.Ringe.
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Ref.
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Science, 1995,
269,
66-69.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine
pancreatic elastase bound to its target serine protease has been solved. The
peptidomimetic molecule binds in the same fashion as the class of dipeptides
from which it was derived, making similar interactions with the subsites on the
elastase surface. Because aminimides are readily synthesized from a wide variety
of starting materials, they form the basis for a combinatorial chemistry
approach to rational drug design.
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Secondary reference #1
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Title
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Structural analysis of the active site of porcine pancreatic elastase based on the X-Ray crystal structures of complexes with trifluoroacetyl-Dipeptide-Anilide inhibitors.
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Authors
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C.Mattos,
D.A.Giammona,
G.A.Petsko,
D.Ringe.
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Ref.
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Biochemistry, 1995,
34,
3193-3203.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Interaction of the peptide cf3-Leu-Ala-Nh-C6h4-Cf3 (tfla) with porcine pancreatic elastase. X-Ray studies at 1.8 angstroms
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Authors
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I.Li de la sierra,
E.Papamichael,
C.Sakarelos,
J.-L.Dimicoli,
T.Prange.
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Ref.
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j mol recog, 1990,
3,
36.
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Secondary reference #3
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Title
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Structure of native porcine pancreatic elastase at 1.65 a resolutions.
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Authors
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E.Meyer,
G.Cole,
R.Radhakrishnan,
O.Epp.
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Ref.
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Acta Crystallogr B, 1988,
44,
26-38.
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PubMed id
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Secondary reference #4
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Title
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Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 a resolution.
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Authors
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E.F.Meyer,
R.Radhakrishnan,
G.M.Cole,
L.G.Presta.
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Ref.
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J Mol Biol, 1986,
189,
533-539.
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PubMed id
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Secondary reference #5
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Title
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Crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastase.
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Authors
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D.L.Hughes,
L.C.Sieker,
J.Bieth,
J.L.Dimicoli.
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Ref.
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J Mol Biol, 1982,
162,
645-658.
[DOI no: ]
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PubMed id
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Figure 1.
FIG. 1. Superposition f the inhibitor molecule and some neighbouring residues on the final difference
map (p,- IF,/) or TFAP in the active site region. Contours ar drawn at estimated lrvrls of 0,;5, I.0 and
1.5 I?.
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Figure 3.
FIG. 3. Th active centre region in: (a) native elastase (pH 5.0); (b) tosyl-elastase; and (c) the
TFAl/elastase complex, TFAP.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #6
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Title
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The indirect mechanism of action of the trifluoroacetyl peptides on elastase. Enzymatic and 19f nmr studies.
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Authors
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J.L.Dimicoli,
A.Renaud,
J.Bieth.
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Ref.
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Eur J Biochem, 1980,
107,
423-432.
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PubMed id
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Secondary reference #7
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Title
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The atomic structure of crystalline porcine pancreatic elastase at 2.5 a resolution: comparisons with the structure of alpha-Chymotrypsin.
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Authors
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L.Sawyer,
D.M.Shotton,
J.W.Campbell,
P.L.Wendell,
H.Muirhead,
H.C.Watson.
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Ref.
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J Mol Biol, 1978,
118,
137-208.
[DOI no: ]
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PubMed id
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Figure 1.
FIG. 1. The variation in he ean arent and heavy-atom structure amplitudes and in he
accurctcy of the hase etermination of the complete high resolution tosyl-elastse data set as a
unction of sin20/ha. (-A-A-), F,//2 -O-O--), lfHl --m--W--, --O--O---,
--A--/--) and E (-m-m--, -e-a--, -b-A-) are defined as in Tables 3 and 4.
The values or wa are iven by the right ordinate, nd those or 1Frl, lfnl and E, which are n he
same non-absolute scale, by the ordinate. A, CMBS-elastase; 0, ranyl tosyl-elastase;
H, uranyl CMBS-elastase.
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Figure 10.
IG. 10. Histograms of (a) x, b) yz, (c) x3.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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