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PDBsum entry 1r8o
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Hydrolase inhibitor
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PDB id
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1r8o
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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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Three-Dimensional structure of an unusual kunitz (sti) type trypsin inhibitor from copaifera langsdorffii.
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Authors
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S.Krauchenco,
R.A.Nagem,
J.A.Da silva,
S.Marangoni,
I.Polikarpov.
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Ref.
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Biochimie, 2004,
86,
167-172.
[DOI no: ]
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PubMed id
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Abstract
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The crystallographic structure of a novel trypsin inhibitor (CTI) from Copaifera
langsdorffii is reported. The structure was solved by MIRAS procedure and
refined to a crystallographic residual of 17.3% (R(free) = 20.3%) at 1.8 A
resolution. Two isomorphous derivatives were obtained by quick cryo-soaking
approach. CTI is the first structure of a member of Kunitz (STI) family formed
by two noncovalently bound polypeptide chains and only one disulfide bridge. A
standard Kunitz-type inhibitor has a single polypeptide chain and two disulfide
bridges. Structural features granting CTI high inhibitory activity are discussed.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction analysis of a novel trypsin inhibitor from seeds of copaifera langsdorffii.
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Authors
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S.Krauchenco,
J.A.Silva,
R.A.Nagem,
J.R.Brandão neto,
V.P.Forrer,
R.Carmona e ferreira,
M.L.Macedo,
J.C.Novello,
S.Marangoni,
I.Polikarpov.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1316-1318.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 Crystals of C. langsdorffii protease inhibitor. The
crystals were grown by the hanging-drop vapour-diffusion method
at 291 K in 0.1 M sodium acetate buffer at pH values near 4
using PEG 4000 (20-25%) as precipitant.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Biochemical characterization and n-Terminal sequences of two new trypsin inhibitors from copaifera langsdorffii seeds.
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Authors
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J.A.Silva,
M.L.Macedo,
J.C.Novello,
S.Marangoni.
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Ref.
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J Protein Chem, 2001,
20,
1-7.
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PubMed id
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