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Proteinase inhibitor (kazal)
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PDB id
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1ovo
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Proteinase inhibitor (kazal)
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Title:
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Crystallographic refinement of japanese quail ovomucoid, a k inhibitor, and model building studies of complexes with ser proteases
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Structure:
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Ovomucoid third domain. Chain: a, b, c, d. Engineered: yes
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Source:
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Coturnix japonica. Japanese quail. Organism_taxid: 93934
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Biol. unit:
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Tetramer (from
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Resolution:
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1.90Å
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R-factor:
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not given
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Authors:
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E.Weber,E.Papamokos,W.Bode,R.Huber,I.Kato,M.Laskowskijunior
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Key ref:
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E.Papamokos
et al.
(1982).
Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.
J Mol Biol,
158,
515-537.
PubMed id:
DOI:
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Date:
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18-Jan-82
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Release date:
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26-May-82
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PROCHECK
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Headers
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References
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P01003
(IOVO_COTJA) -
Ovomucoid
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Seq: Struc:
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186 a.a.
56 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Gene Ontology (GO) functional annotation
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Biochemical function
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protein binding
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2 terms
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DOI no:
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J Mol Biol
158:515-537
(1982)
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PubMed id:
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Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.
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E.Papamokos,
E.Weber,
W.Bode,
R.Huber,
M.W.Empie,
I.Kato,
M.Laskowski.
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ABSTRACT
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Selected figure(s)
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Figure 2.
IG:. 2. St,rreo drawing of the C'' and side -chain arrangement of OMJl'Q3 (m&rule 1)
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Figure 5.
FIG:. 5. )istril)ution of B-values of molecnlrs 1 ( x ) and 1 (0) (a). The B-values of t,he main-chains
wew plotted after avraging the individual VHIIIVS of C'``. Co. S. (`. 0 for each residur. (t)) Thr sarw for
molrcllles 3 ( x ) nd 4 (0).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1982,
158,
515-537)
copyright 1982.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
|
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A.Berchanski,
B.Shapira,
and
M.Eisenstein
(2004).
Hydrophobic complementarity in protein-protein docking.
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| |
Proteins, 56,
130-142.
|
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|
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|
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A.Heifetz,
E.Katchalski-Katzir,
and
M.Eisenstein
(2002).
Electrostatics in protein-protein docking.
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Protein Sci, 11,
571-587.
|
 |
|
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|
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H.Hemmi,
T.Yoshida,
T.Kumazaki,
N.Nemoto,
J.Hasegawa,
F.Nishioka,
Y.Kyogoku,
H.Yokosawa,
and
Y.Kobayashi
(2002).
Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy.
|
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Biochemistry, 41,
10657-10664.
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PDB code:
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S.Ye,
A.L.Cech,
R.Belmares,
R.C.Bergstrom,
Y.Tong,
D.R.Corey,
M.R.Kanost,
and
E.J.Goldsmith
(2001).
The structure of a Michaelis serpin-protease complex.
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Nat Struct Biol, 8,
979-983.
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PDB codes:
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W.R.Forsyth,
and
A.D.Robertson
(2000).
Insensitivity of perturbed carboxyl pK(a) values in the ovomucoid third domain to charge replacement at a neighboring residue.
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Biochemistry, 39,
8067-8072.
|
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J.A.Cuff,
and
G.J.Barton
(1999).
Evaluation and improvement of multiple sequence methods for protein secondary structure prediction.
|
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Proteins, 34,
508-519.
|
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|
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|
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J.Li,
Z.Wang,
B.Canagarajah,
H.Jiang,
M.Kanost,
and
E.J.Goldsmith
(1999).
The structure of active serpin 1K from Manduca sexta.
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Structure, 7,
103-109.
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PDB code:
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J.Liu,
Y.Gong,
O.Prakash,
L.Wen,
I.Lee,
J.K.Huang,
and
R.Krishnamoorthi
(1998).
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
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Protein Sci, 7,
132-141.
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T.Asao,
K.Takahashi,
and
M.Tashiro
(1998).
Interaction of second and third domains of Japanese quail ovomucoid with ten mammalian trypsins.
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Biochim Biophys Acta, 1387,
415-421.
|
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C.Chothia,
T.Hubbard,
S.Brenner,
H.Barns,
and
A.Murzin
(1997).
Protein folds in the all-beta and all-alpha classes.
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Annu Rev Biophys Biomol Struct, 26,
597-627.
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K.Huang,
W.Lu,
S.Anderson,
M.Laskowski,
and
M.N.James
(1995).
Water molecules participate in proteinase-inhibitor interactions: crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B.
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Protein Sci, 4,
1985-1997.
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PDB codes:
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D.V.Laurents,
S.Subbiah,
and
M.Levitt
(1994).
Different protein sequences can give rise to highly similar folds through different stabilizing interactions.
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Protein Sci, 3,
1938-1944.
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|
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E.J.Goldsmith,
and
J.Mottonen
(1994).
Serpins: the uncut version.
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Structure, 2,
241-244.
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|
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K.Huang,
N.C.Strynadka,
V.D.Bernard,
R.J.Peanasky,
and
M.N.James
(1994).
The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase.
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Structure, 2,
679-689.
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PDB code:
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S.Bromberg,
and
K.A.Dill
(1994).
Side-chain entropy and packing in proteins.
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Protein Sci, 3,
997.
|
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|
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|
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G.Müller,
M.Gurrath,
M.Kurz,
and
H.Kessler
(1993).
Beta VI turns in peptides and proteins: a model peptide mimicry.
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| |
Proteins, 15,
235-251.
|
 |
|
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|
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P.C.Sil,
T.K.Chaudhuri,
and
N.K.Sinha
(1993).
Basic trypsin-subtilisin inhibitor from marine turtle egg white: hydrodynamic and inhibitory properties.
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| |
J Protein Chem, 12,
71-78.
|
 |
|
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|
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W.Bode,
and
R.Huber
(1992).
Natural protein proteinase inhibitors and their interaction with proteinases.
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| |
Eur J Biochem, 204,
433-451.
|
 |
|
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|
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S.D.Patterson,
K.Bell,
and
D.C.Shaw
(1991).
The equine major plasma serpin multigene family: partial characterization including sequence of the reactive-site regions.
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| |
Biochem Genet, 29,
477-499.
|
 |
|
|
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|
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M.Bolognesi,
L.Pugliese,
G.Gatti,
F.Frigerio,
A.Coda,
L.Antolini,
H.P.Schnebli,
E.Menegatti,
G.Amiconi,
and
P.Ascenzi
(1990).
X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution.
|
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J Mol Recognit, 3,
163-168.
|
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|
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G.M.Clore,
and
A.M.Gronenborn
(1989).
Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy.
|
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Crit Rev Biochem Mol Biol, 24,
479-564.
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|
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R.Wang,
R.J.Cotter,
T.Y.Lin,
and
M.Laskowski
(1988).
Plasma desorption mass spectrometric analysis of glycosylated ovomucoid third domain from Japanese quail.
|
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Rapid Commun Mass Spectrom, 2,
71-73.
|
 |
|
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|
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L.G.Presta,
and
E.F.Meyer
(1987).
Prediction of protein--ligand interactions: the complex of porcine pancreatic elastase with a valine-derived benzoxazinone.
|
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Biopolymers, 26,
1207-1225.
|
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|
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|
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W.Bode,
E.Papamokos,
and
D.Musil
(1987).
The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.
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Eur J Biochem, 166,
673-692.
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PDB code:
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|
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W.Braun
(1987).
Distance geometry and related methods for protein structure determination from NMR data.
|
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Q Rev Biophys, 19,
115-157.
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|
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J.J.Beintema
(1986).
Do asparagine-linked carbohydrate chains in glycoproteins have a preference for beta-bends?
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Biosci Rep, 6,
709-714.
|
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|
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|
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J.L.Markley,
D.H.Croll,
R.Krishnamoorthi,
G.Ortiz-Polo,
W.M.Westler,
W.C.Bogard,
and
M.Laskowski
(1986).
One- and two-dimensional NMR spectral analysis of the consequences of single amino acid replacements in proteins.
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J Cell Biochem, 30,
291-309.
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W.Bode,
A.Z.Wei,
R.Huber,
E.Meyer,
J.Travis,
and
S.Neumann
(1986).
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.
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EMBO J, 5,
2453-2458.
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PDB code:
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W.Bode,
E.Papamokos,
D.Musil,
U.Seemueller,
and
H.Fritz
(1986).
Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.
|
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EMBO J, 5,
813-818.
|
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|
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C.A.McPhalen,
I.Svendsen,
I.Jonassen,
and
M.N.James
(1985).
Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin Novo.
|
| |
Proc Natl Acad Sci U S A, 82,
7242-7246.
|
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|
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W.Bode,
O.Epp,
R.Huber,
M.Laskowski,
and
W.Ardelt
(1985).
The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).
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| |
Eur J Biochem, 147,
387-395.
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PDB code:
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R.Huber,
and
W.S.Bennett
(1983).
Functional significance of flexibility in proteins.
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Biopolymers, 22,
261-279.
|
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|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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