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PDBsum entry 8api
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Proteinase inhibitor
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PDB id
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8api
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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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The s variant of human alpha 1-Antitrypsin, Structure and implications for function and metabolism.
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Authors
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R.Engh,
H.Löbermann,
M.Schneider,
G.Wiegand,
R.Huber,
C.B.Laurell.
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Ref.
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Protein Eng, 1989,
2,
407-415.
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PubMed id
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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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Secondary reference #1
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Title
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Human alpha 1-Proteinase inhibitor. Crystal structure analysis of two crystal modifications, Molecular model and preliminary analysis of the implications for function.
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Authors
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H.Loebermann,
R.Tokuoka,
J.Deisenhofer,
R.Huber.
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Ref.
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J Mol Biol, 1984,
177,
531-557.
[DOI no: ]
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PubMed id
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Figure 4.
IG. 4. (a) and (b) Stereo diagram of the arrangement of sheets A to C. (Figs 3(b), 3(c), 4(b) and 5
were produced with a program by Lesk & Hardman (1982).)
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Figure 6.
FIG. 6. Stereo diagrams of the distribution of (a) apolar, (1)) acidic and (c) basic residues in
cc,-proteinase inhibitor.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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Interaction of human alpha 1-Proteinase inhibitor with chymotrypsinogen a and crystallization of a proteolytically modified alpha 1-Proteinase inhibitor.
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Authors
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H.Löbermann,
F.Lottspeich,
W.Bode,
R.Huber.
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Ref.
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Hoppe Seylers Z Physiol Chem, 1982,
363,
1377-1388.
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PubMed id
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Secondary reference #3
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Title
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The biosynthesis of rat alpha 1-Antitrypsin.
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Authors
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J.Carlson,
J.Stenflo.
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Ref.
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J Biol Chem, 1982,
257,
12987-12994.
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PubMed id
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Secondary reference #4
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Title
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Human alpha 1-Antitrypsin: carbohydrate attachment and sequence homology.
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Authors
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R.W.Carrell,
J.O.Jeppsson,
L.Vaughan,
S.O.Brennan,
M.C.Owen,
D.R.Boswell.
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Ref.
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Febs Lett, 1981,
135,
301-303.
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PubMed id
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Secondary reference #5
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Title
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Studies on the oligosaccharide chains of human alpha 1-Protease inhibitor. Ii. Structure of oligosaccharides.
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Authors
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T.Mega,
E.Lujan,
A.Yoshida.
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Ref.
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J Biol Chem, 1980,
255,
4057-4061.
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PubMed id
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