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PDBsum entry 1tus
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Serine proteinase inhibitor
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PDB id
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1tus
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Contents |
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* Residue conservation analysis
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J Mol Biol
242:215-230
(1994)
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PubMed id:
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Solution structure of reactive-site hydrolyzed turkey ovomucoid third domain by nuclear magnetic resonance and distance geometry methods.
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W.F.Walkenhorst,
A.M.Krezel,
G.I.Rhyu,
J.L.Markley.
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ABSTRACT
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The solution structure of reactive-site hydrolyzed turkey ovomucoid third domain
(OMTKY3*) was determined by n.m.r. methods. A total of 655 distance constraints
was applied in a distance geometry/simulated annealing approach to calculate a
family of structures consistent with the n.m.r. data. The input data included 24
torsion angle constraints, 14 hydrogen bonds, 611 constraints derived from
two-dimensional nuclear Overhauser enhancement spectroscopy data, and three
disulfide bridges. Stereospecific assignments were included for the hydrogens of
26 beta-methylene groups and for seven isopropyl methyl groups (46% chiral
assignments). OMTKY3* in solution retains the global fold and overall secondary
structure of the intact inhibitor (OMTKY3) but exhibits local structural
differences at and adjacent to the clip site. In particular, the
hydrogen-bonding network observed at the reactive-site of the intact inhibitor
is disrupted, and the position of Tyr20 is altered in the modified inhibitor. No
evidence was found for ion pairing between the oppositely charged termini at the
clip site. Surprisingly, in light of numerous changes indicating that OMTKY3* is
less stable than OMTKY3, rotation of the Tyr31 ring was found to be slow in
OMTKY3* at 30 degrees C. In OMTKY3, slow rotation of the Tyr31 ring was observed
only at temperatures below 15 degrees C. The n.m.r. structures of OMTKY3* are
compared here with the similarly calculated structures of OMTKY3. This
represents the first comparison of an intact and modified (reactive-site
clipped) proteinase inhibitor under identical conditions. On comparison with
published X-ray structures of modified avian ovomucoid third domains from two
other species, the present structure of OMTKY3* in solution was found to
resemble that of the Japanese quail protein (OMJPQ3*) more closely than that of
the more closely homologous silver pheasant protein (OMSVP3*).
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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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O.Buczek,
D.Krowarsch,
and
J.Otlewski
(2002).
Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).
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Protein Sci,
11,
924-932.
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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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C.G.Hoogstraten,
S.Choe,
W.M.Westler,
and
J.L.Markley
(1995).
Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data.
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Protein Sci,
4,
2289-2299.
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PDB codes:
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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
codes are
shown on the right.
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Links
