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PDBsum entry 7api
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Proteinase inhibitor
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PDB id
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7api
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Contents |
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* Residue conservation analysis
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Protein Eng
2:407-415
(1989)
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PubMed id:
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The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.
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R.Engh,
H.Löbermann,
M.Schneider,
G.Wiegand,
R.Huber,
C.B.Laurell.
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ABSTRACT
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The S variant of the human alpha 1-antitrypsin with E-264----V, is responsible
for a mild alpha 1-antitrypsin deficiency quite common in the European
population. S protein specifically cleaved at the susceptible peptide bond was
crystallized and its crystal structure determined and refined to 3.1 A
resolution. The S variant crystallizes isomorphous to the normal M variant. The
difference Fourier electron density map shows the E----V change as outstanding
residual density. In addition, small structural changes of the main polypeptide
chain radiate from the site of mutation and affect parts far removed from it. By
the mutation, internal hydrogen bonds and salt linkages of E-264 to Y-38 and
K-487, respectively, are lost. They cause the far-reaching slight distortions
and are probably related to the reduced thermal stability of the S mutant. They
may also be responsible for slower folding of the polypeptide chain and the
clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by
molecular dynamics methods simulations of the M and S proteins were made and the
results analysed with respect to structural and dynamic properties and compared
with the experimental results. There is a significant correlation between
experimental and theoretical results in some respects.
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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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M.J.Bennett,
M.R.Sawaya,
and
D.Eisenberg
(2006).
Deposition diseases and 3D domain swapping.
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Structure,
14,
811-824.
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T.Wind,
J.K.Jensen,
D.M.Dupont,
P.Kulig,
and
P.A.Andreasen
(2003).
Mutational analysis of plasminogen activator inhibitor-1.
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Eur J Biochem,
270,
1680-1688.
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P.R.Elliott,
X.Y.Pei,
T.R.Dafforn,
and
D.A.Lomas
(2000).
Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease.
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Protein Sci,
9,
1274-1281.
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PDB code:
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P.R.Elliott,
P.E.Stein,
D.Bilton,
R.W.Carrell,
and
D.A.Lomas
(1996).
Structural explanation for the deficiency of S alpha 1-antitrypsin.
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Nat Struct Biol,
3,
910-911.
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T.Samandari,
and
J.L.Brown
(1993).
A study of the effects of altering the sites for N-glycosylation in alpha-1-proteinase inhibitor variants M and S.
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Protein Sci,
2,
1400-1410.
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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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N.Kalsheker,
and
K.Morgan
(1990).
Molecular biology and respiratory disease. 7. The alpha 1 antitrypsin gene and chronic lung disease.
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Thorax,
45,
759-764.
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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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Links
