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PDBsum entry 6api

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Proteinase inhibitor PDB id
6api

 

 

 

 

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Contents
Protein chains
339 a.a.
35 a.a.
Ligands
GTH
NAG-NAG-MAN-MAN-
NAG-MAN
NAG-NAG
NAG
Waters ×49
Superseded by: 8api 8api
PDB id:
6api
Name: Proteinase inhibitor
Structure: Modified alpha=1=- Antitrypsin (modified alpha=1=- Proteinase inhibitor)
Source: Human (homo sapiens)
Authors: H.Loebermann,R.Tokuoka,J.Deisenhofer,R.Huber
Key ref:
H.Loebermann et al. (1984). Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol, 177, 531-557. PubMed id: 6332197 DOI: 10.1016/0022-2836(84)90298-5
Date:
22-Oct-84     Release date:   29-Oct-84    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 339 a.a.
Protein chain
No UniProt id for this chain
Struc: 35 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1016/0022-2836(84)90298-5 J Mol Biol 177:531-557 (1984)
PubMed id: 6332197  
 
 
Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function.
H.Loebermann, R.Tokuoka, J.Deisenhofer, R.Huber.
 
  ABSTRACT  
 
Two closely related crystal structures of alpha 1-proteinase inhibitor modified at the reactive site peptide bond Met358--Ser359 have been analysed. The crystal structure has been obtained from diffraction data at 3 A resolution, with phases originally from isomorphous replacement. The electron density map was substantially improved by cyclic averaging of the electron densities of the two crystal forms and allowed the chain to be traced in terms of the known chemical amino acid sequence. Energy restrained crystallographic refinement was initiated and resulted in conventional R-values of 0.251 for the tetragonal crystal form (6 to 3 A resolution) and 0.247 for the hexagonal crystal form (6 to 3.2 A resolution). The polypeptide chain is almost completely arranged in well-defined secondary structural elements: three beta-sheets and eight alpha-helices. The helices are preferentially formed by the first 150 residues. They are in proximity underneath sheet A. The chain ends Met358 and Ser359 of the nicked species are arranged in strands on opposite ends of the molecule indicating a major structural rearrangement upon modification of the intact inhibitor. It is suggested that the Met358 strand is in a different conformation removed from sheet A and approaches Ser359 in the intact inhibitor species. Glu342, which is exchanged by a lysine in the Z-variant is in a strategic position for such a rearrangement. The three carbohydrate chains of alpha 1-proteinase inhibitor have partly defined electron density close to their attachment sites at asparagine residues. The anti-thrombin and ovalbumin amino acid sequences can be accommodated in the alpha 1 inhibitor molecular structure. The intron-exon junctions of the ovalbumin and the alpha 1-proteinase inhibitor gene are all in surface loops of the mature protein.
 
  Selected figure(s)  
 
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).)
Figure 6.
FIG. 6. Stereo diagrams of the distribution of (a) apolar, (1)) acidic and (c) basic residues in cc,-proteinase inhibitor.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1984, 177, 531-557) copyright 1984.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19893573 D.Kaiserman, and P.I.Bird (2010).
Control of granzymes by serpins.
  Cell Death Differ, 17, 586-595.  
20731544 J.A.Huntington, and J.C.Whisstock (2010).
Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.
  Biol Chem, 391, 973-982.  
20180638 J.E.Swedberg, S.J.de Veer, and J.M.Harris (2010).
Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia.
  Biol Chem, 391, 357-374.  
19245336 B.Gooptu, and D.A.Lomas (2009).
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
  Annu Rev Biochem, 78, 147-176.  
19492109 C.Boudier, A.S.Klymchenko, Y.Mely, and A.Follenius-Wund (2009).
Local environment perturbations in alpha(1)-antitrypsin monitored by a ratiometric fluorescent label.
  Photochem Photobiol Sci, 8, 814-821.  
19298613 S.Jesse, P.Steinacker, S.Lehnert, F.Gillardon, B.Hengerer, and M.Otto (2009).
Neurochemical approaches in the laboratory diagnosis of Parkinson and Parkinson dementia syndromes: a review.
  CNS Neurosci Ther, 15, 157-182.  
19120695 Y.P.Chang, R.Mahadeva, W.S.Chang, S.C.Lin, and Y.H.Chu (2009).
Small-molecule peptides inhibit Z alpha1-antitrypsin polymerization.
  J Cell Mol Med, 13, 2304-2316.  
17917376 C.Yamagishi, Y.Momoi, T.Kobayashi, K.Ide, K.Ohno, H.Tsujimoto, and T.Iwasaki (2007).
A retrospective study and gene analysis of canine sterile panniculitis.
  J Vet Med Sci, 69, 915-924.  
17660256 J.H.Baek, H.Im, U.B.Kang, K.M.Seong, C.Lee, J.Kim, and M.H.Yu (2007).
Probing the local conformational change of alpha1-antitrypsin.
  Protein Sci, 16, 1842-1850.  
17442346 P.Chowdhury, W.Wang, S.Lavender, M.R.Bunagan, J.W.Klemke, J.Tang, J.G.Saven, B.S.Cooperman, and F.Gai (2007).
Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides.
  J Mol Biol, 369, 462-473.  
17393427 Z.Ding, F.Qu, W.Guo, X.Ying, M.Wu, and Y.Zhang (2007).
Identification of sperm forward motility-related proteins in human seminal plasma.
  Mol Reprod Dev, 74, 1124-1131.  
16938877 A.Zhou, Z.Wei, R.J.Read, and R.W.Carrell (2006).
Structural mechanism for the carriage and release of thyroxine in the blood.
  Proc Natl Acad Sci U S A, 103, 13321-13326.
PDB code: 2ceo
16627467 D.Ivanov, C.Emonet, F.Foata, M.Affolter, M.Delley, M.Fisseha, S.Blum-Sperisen, S.Kochhar, and F.Arigoni (2006).
A serpin from the gut bacterium Bifidobacterium longum inhibits eukaryotic elastase-like serine proteases.
  J Biol Chem, 281, 17246-17252.  
16773239 E.Karnaukhova, Y.Ophir, and B.Golding (2006).
Recombinant human alpha-1 proteinase inhibitor: towards therapeutic use.
  Amino Acids, 30, 317-332.  
16820297 J.A.Huntington (2006).
Shape-shifting serpins--advantages of a mobile mechanism.
  Trends Biochem Sci, 31, 427-435.  
16698543 M.J.Bennett, M.R.Sawaya, and D.Eisenberg (2006).
Deposition diseases and 3D domain swapping.
  Structure, 14, 811-824.  
16737556 R.H.Law, Q.Zhang, S.McGowan, A.M.Buckle, G.A.Silverman, W.Wong, C.J.Rosado, C.G.Langendorf, R.N.Pike, P.I.Bird, and J.C.Whisstock (2006).
An overview of the serpin superfamily.
  Genome Biol, 7, 216.  
15653733 C.Boudier, A.Gils, P.J.Declerck, and J.G.Bieth (2005).
The conversion of active to latent plasminogen activator inhibitor-1 is an energetically silent event.
  Biophys J, 88, 2848-2854.  
15914911 N.Takahashi, M.Onda, K.Hayashi, M.Yamasaki, T.Mita, and M.Hirose (2005).
Thermostability of refolded ovalbumin and S-ovalbumin.
  Biosci Biotechnol Biochem, 69, 922-931.  
16052629 R.L.Moritz, A.B.Clippingdale, E.A.Kapp, J.S.Eddes, H.Ji, S.Gilbert, L.M.Connolly, and R.J.Simpson (2005).
Application of 2-D free-flow electrophoresis/RP-HPLC for proteomic analysis of human plasma depleted of multi high-abundance proteins.
  Proteomics, 5, 3402-3413.  
15892855 W.Bode (2005).
The structure of thrombin, a chameleon-like proteinase.
  J Thromb Haemost, 3, 2379-2388.  
14767073 C.H.Jung, Y.R.Na, and H.Im (2004).
Retarded protein folding of deficient human alpha 1-antitrypsin D256V and L41P variants.
  Protein Sci, 13, 694-702.  
15486938 S.Janciauskiene, S.Eriksson, F.Callea, M.Mallya, A.Zhou, K.Seyama, S.Hata, and D.A.Lomas (2004).
Differential detection of PAS-positive inclusions formed by the Z, Siiyama, and Mmalton variants of alpha1-antitrypsin.
  Hepatology, 40, 1203-1210.  
15638455 T.H.Roberts, J.Hejgaard, N.F.Saunders, R.Cavicchioli, and P.M.Curmi (2004).
Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution.
  J Mol Evol, 59, 437-447.  
12578831 A.Zhou, P.E.Stein, J.A.Huntington, and R.W.Carrell (2003).
Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol.
  J Biol Chem, 278, 15116-15122.
PDB code: 1lk6
12671072 D.T.Berg, B.Gerlitz, J.Shang, T.Smith, P.Santa, M.A.Richardson, K.D.Kurz, B.W.Grinnell, K.Mace, and B.E.Jones (2003).
Engineering the proteolytic specificity of activated protein C improves its pharmacological properties.
  Proc Natl Acad Sci U S A, 100, 4423-4428.  
12649292 E.Marszal, D.Danino, and A.Shrake (2003).
A novel mode of polymerization of alpha1-proteinase inhibitor.
  J Biol Chem, 278, 19611-19618.  
12834280 F.Tani, N.Shirai, Y.Nakanishi, and N.Kitabatake (2003).
Analysis of molecular interactions in heat-induced aggregation of a non-inhibitory serpin ovalbumin using a molecular chaperone.
  Biosci Biotechnol Biochem, 67, 1030-1038.  
12784625 H.Yamamoto, N.Takahashi, M.Yamasaki, Y.Arii, and M.Hirose (2003).
Thermostabilization of ovalbumin by an alkaline treatment: examination for the possible implications of an altered serpin loop structure.
  Biosci Biotechnol Biochem, 67, 830-837.  
12871289 J.A.Huntington (2003).
Mechanisms of glycosaminoglycan activation of the serpins in hemostasis.
  J Thromb Haemost, 1, 1535-1549.  
12682008 M.Wilczynska, S.Lobov, P.I.Ohlsson, and T.Ny (2003).
A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerization.
  EMBO J, 22, 1753-1761.  
12956655 P.Petropoulou, Z.Zhang, M.A.Curtis, N.W.Johnson, F.J.Hughes, and P.G.Winyard (2003).
Measurement of both native and inactivated forms of alpha1 proteinase inhibitor in human inflammatory extracellular fluids.
  J Clin Periodontol, 30, 795-801.  
12223472 A.A.Komissarov, P.J.Declerck, and J.D.Shore (2002).
Mechanisms of conversion of plasminogen activator inhibitor 1 from a suicide inhibitor to a substrate by monoclonal antibodies.
  J Biol Chem, 277, 43858-43865.  
11834734 E.J.Seo, C.Lee, and M.H.Yu (2002).
Concerted regulation of inhibitory activity of alpha 1-antitrypsin by the native strain distributed throughout the molecule.
  J Biol Chem, 277, 14216-14220.  
11986314 J.E.Chipuk, L.V.Stewart, A.Ranieri, K.Song, and D.Danielpour (2002).
Identification and characterization of a novel rat ov-serpin family member, trespin.
  J Biol Chem, 277, 26412-26421.  
11159419 J.P.Ludeman, J.C.Whisstock, P.C.Hopkins, B.F.Le Bonniec, and S.P.Bottomley (2001).
Structure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopy.
  Biophys J, 80, 491-497.  
11546761 L.Jankova, S.J.Harrop, D.N.Saunders, J.L.Andrews, K.C.Bertram, A.R.Gould, M.S.Baker, and P.M.Curmi (2001).
Crystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loop.
  J Biol Chem, 276, 43374-43382.
PDB code: 1jrr
11767949 M.K.Chow, G.L.Devlin, and S.P.Bottomley (2001).
Osmolytes as modulators of conformational changes in serpins.
  Biol Chem, 382, 1593-1599.  
11683637 S.J.Riedl, M.Renatus, S.J.Snipas, and G.S.Salvesen (2001).
Mechanism-based inactivation of caspases by the apoptotic suppressor p35.
  Biochemistry, 40, 13274-13280.  
11278163 S.Janciauskiene (2001).
Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles.
  Biochim Biophys Acta, 1535, 221-235.  
11685246 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.
  Nat Struct Biol, 8, 979-983.
PDB codes: 1i99 1k9o
  11063688 C.Green, E.Levashina, C.McKimmie, T.Dafforn, J.M.Reichhart, and D.Gubb (2000).
The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2.
  Genetics, 156, 1117-1127.  
10681574 D.A.Lawrence, S.T.Olson, S.Muhammad, D.E.Day, J.O.Kvassman, D.Ginsburg, and J.D.Shore (2000).
Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.
  J Biol Chem, 275, 5839-5844.  
  10718550 G.C.Schussler (2000).
The thyroxine-binding proteins.
  Thyroid, 10, 141-149.  
  10975571 H.Im, H.Y.Ahn, and M.H.Yu (2000).
Bypassing the kinetic trap of serpin protein folding by loop extension.
  Protein Sci, 9, 1497-1502.  
10954248 J.H.Lee, and M.Brantly (2000).
Molecular mechanisms of alpha1-antitrypsin null alleles.
  Respir Med, 94, S7-11.  
  10716194 M.A.Dunstone, W.Dai, J.C.Whisstock, J.Rossjohn, R.N.Pike, S.C.Feil, B.F.Le Bonniec, M.W.Parker, and S.P.Bottomley (2000).
Cleaved antitrypsin polymers at atomic resolution.
  Protein Sci, 9, 417-420.
PDB code: 1d5s
10801484 M.Fa, F.Bergström, P.Hägglöf, M.Wilczynska, L.B.Johansson, and T.Ny (2000).
The structure of a serpin-protease complex revealed by intramolecular distance measurements using donor-donor energy migration and mapping of interaction sites.
  Structure, 8, 397-405.  
10903953 M.Renatus, Q.Zhou, H.R.Stennicke, S.J.Snipas, D.Turk, L.A.Bankston, R.C.Liddington, and G.S.Salvesen (2000).
Crystal structure of the apoptotic suppressor CrmA in its cleaved form.
  Structure, 8, 789-797.
PDB code: 1f0c
10753871 P.Mellet, and J.G.Bieth (2000).
Evidence that translocation of the proteinase precedes its acylation in the serpin inhibition pathway.
  J Biol Chem, 275, 10788-10795.  
  10933492 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.
  Protein Sci, 9, 1274-1281.
PDB code: 1qlp
10913307 S.R.Hwang, B.Steineckert, and V.Y.Hook (2000).
Expression and mutagenesis of the novel serpin endopin 2 demonstrates a requirement for cysteine-374 for dithiothreitol-sensitive inhibition of elastase.
  Biochemistry, 39, 8944-8952.  
11123897 S.Yakovlev, S.Litvinovich, D.Loukinov, and L.Medved (2000).
Role of the beta-strand insert in the central domain of the fibrinogen gamma-module.
  Biochemistry, 39, 15721-15729.  
10368279 A.M.Sharp, P.E.Stein, N.S.Pannu, R.W.Carrell, M.B.Berkenpas, D.Ginsburg, D.A.Lawrence, and R.J.Read (1999).
The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion.
  Structure, 7, 111-118.
PDB code: 1b3k
10092631 E.L.James, J.C.Whisstock, M.G.Gore, and S.P.Bottomley (1999).
Probing the unfolding pathway of alpha1-antitrypsin.
  J Biol Chem, 274, 9482-9488.  
10196190 H.Im, E.J.Seo, and M.H.Yu (1999).
Metastability in the inhibitory mechanism of human alpha1-antitrypsin.
  J Biol Chem, 274, 11072-11077.  
10373004 J.C.Whisstock, J.A.Irving, S.P.Bottomley, R.N.Pike, and A.M.Lesk (1999).
Serpins in the Caenorhabditis elegans genome.
  Proteins, 36, 31-41.  
10368276 J.Li, Z.Wang, B.Canagarajah, H.Jiang, M.Kanost, and E.J.Goldsmith (1999).
The structure of active serpin 1K from Manduca sexta.
  Structure, 7, 103-109.
PDB code: 1sek
10368272 S.J.Harrop, L.Jankova, M.Coles, D.Jardine, J.S.Whittaker, A.R.Gould, A.Meister, G.C.King, B.C.Mabbutt, and P.M.Curmi (1999).
The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: implications for serpin function.
  Structure, 7, 43-54.
PDB code: 1by7
10092640 T.R.Dafforn, R.Mahadeva, P.R.Elliott, P.Sivasothy, and D.A.Lomas (1999).
A kinetic mechanism for the polymerization of alpha1-antitrypsin.
  J Biol Chem, 274, 9548-9555.  
9988693 V.Picard, P.E.Marque, F.Paolucci, M.Aiach, and B.F.Le Bonniec (1999).
Topology of the stable serpin-protease complexes revealed by an autoantibody that fails to react with the monomeric conformers of antithrombin.
  J Biol Chem, 274, 4586-4593.  
10089448 W.Huang, T.A.Haas, J.Biesterfeldt, L.Mankawsky, R.E.Blanton, and X.Lee (1999).
Purification and crystallization of a novel membrane-anchored protein: the Schistosoma haematobium serpin.
  Acta Crystallogr D Biol Crystallogr, 55, 350-352.  
9468513 C.E.Chaillan-Huntington, and P.A.Patston (1998).
Influence of the P5 residue on alpha1-proteinase inhibitor mechanism.
  J Biol Chem, 273, 4569-4573.  
9799512 J.O.Kvassman, I.Verhamme, and J.D.Shore (1998).
Inhibitory mechanism of serpins: loop insertion forces acylation of plasminogen activator by plasminogen activator inhibitor-1.
  Biochemistry, 37, 15491-15502.  
9442015 J.R.Dahlen, F.Jean, G.Thomas, D.C.Foster, and W.Kisiel (1998).
Inhibition of soluble recombinant furin by human proteinase inhibitor 8.
  J Biol Chem, 273, 1851-1854.  
9538691 J.Whisstock, R.Skinner, and A.M.Lesk (1998).
An atlas of serpin conformations.
  Trends Biochem Sci, 23, 63-67.  
9446551 K.N.Lee, H.Im, S.W.Kang, and M.H.Yu (1998).
Characterization of a human alpha1-antitrypsin variant that is as stable as ovalbumin.
  J Biol Chem, 273, 2509-2516.  
9535901 P.Mellet, C.Boudier, Y.Mely, and J.G.Bieth (1998).
Stopped flow fluorescence energy transfer measurement of the rate constants describing the reversible formation and the irreversible rearrangement of the elastase-alpha1-proteinase inhibitor complex.
  J Biol Chem, 273, 9119-9123.  
9452500 W.S.Chang, and D.A.Lomas (1998).
Latent alpha1-antichymotrypsin. A molecular explanation for the inactivation of alpha1-antichymotrypsin in chronic bronchitis and emphysema.
  J Biol Chem, 273, 3695-3701.  
9236002 C.E.Chaillan-Huntington, P.G.Gettins, J.A.Huntington, and P.A.Patston (1997).
The P6-P2 region of serpins is critical for proteinase inhibition and complex stability.
  Biochemistry, 36, 9562-9570.  
9145100 D.A.Lawrence (1997).
The serpin-proteinase complex revealed.
  Nat Struct Biol, 4, 339-341.  
9235938 E.Ersdal-Badju, A.Lu, Y.Zuo, V.Picard, and S.C.Bock (1997).
Identification of the antithrombin III heparin binding site.
  J Biol Chem, 272, 19393-19400.  
9154928 G.Kaslik, J.Kardos, E.Szabó, L.Szilágyi, P.Závodszky, W.M.Westler, J.L.Markley, and L.Gráf (1997).
Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site.
  Biochemistry, 36, 5455-5464.  
  9285829 G.P.Briley, M.A.Hissong, M.L.Chiu, and D.C.Lee (1997).
The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing.
  Mol Biol Cell, 8, 1619-1631.  
9120024 I.Inoue, T.Nakajima, C.S.Williams, J.Quackenbush, R.Puryear, M.Powers, T.Cheng, E.H.Ludwig, A.M.Sharma, A.Hata, X.Jeunemaitre, and J.M.Lalouel (1997).
A nucleotide substitution in the promoter of human angiotensinogen is associated with essential hypertension and affects basal transcription in vitro.
  J Clin Invest, 99, 1786-1797.  
9402754 J.R.Dahlen, D.C.Foster, and W.Kisiel (1997).
Expression, purification, and inhibitory properties of human proteinase inhibitor.
  Biochemistry, 36, 14874-14882.  
9405673 L.Jin, J.P.Abrahams, R.Skinner, M.Petitou, R.N.Pike, and R.W.Carrell (1997).
The anticoagulant activation of antithrombin by heparin.
  Proc Natl Acad Sci U S A, 94, 14683-14688.
PDB code: 1azx
9145103 M.Wilczynska, M.Fa, J.Karolin, P.I.Ohlsson, L.B.Johansson, and T.Ny (1997).
Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins.
  Nat Struct Biol, 4, 354-357.  
9020092 P.C.Hopkins, W.S.Chang, M.R.Wardell, and S.R.Stone (1997).
Inhibitory mechanism of serpins. Mobility of the C-terminal region of the reactive-site loop.
  J Biol Chem, 272, 3905-3909.  
9148970 P.Choudhury, Y.Liu, R.J.Bick, and R.N.Sifers (1997).
Intracellular association between UDP-glucose:glycoprotein glucosyltransferase and an incompletely folded variant of alpha1-antitrypsin.
  J Biol Chem, 272, 13446-13451.  
8652525 A.Gils, I.Knockaert, and P.J.Declerck (1996).
Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop.
  Biochemistry, 35, 7474-7481.  
8856053 A.J.Schulze, D.Quarzago, and P.A.Andreasen (1996).
A spectroscopic study of the structures of latent, active and reactive-center-cleaved type-1 plasminogen-activator inhibitor.
  Eur J Biochem, 240, 550-555.  
  8732755 B.O.Villoutreix, H.Lilja, K.Pettersson, T.Lövgren, and O.Teleman (1996).
Structural investigation of the alpha-1-antichymotrypsin: prostate-specific antigen complex by comparative model building.
  Protein Sci, 5, 836-851.  
8836107 C.M.Lukacs, J.Q.Zhong, M.I.Plotnick, H.Rubin, B.S.Cooperman, and D.W.Christianson (1996).
Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement.
  Nat Struct Biol, 3, 888-893.
PDB codes: 1ct3 2caa
8813337 D.A.Lane, G.Kunz, R.J.Olds, and S.L.Thein (1996).
Molecular genetics of antithrombin deficiency.
  Blood Rev, 10, 59-74.  
8895089 H.Koloczek, A.Guz, and P.Kaszycki (1996).
Fluorescence-detected polymerization kinetics of human alpha 1-antitrypsin.
  J Protein Chem, 15, 447-454.  
8620872 H.M.Tucker, and R.D.Gerard (1996).
Sequence requirements in the reactive-center loop of plasminogen-activator inhibitor-1 for recognition of plasminogen activators.
  Eur J Biochem, 237, 180-187.  
8703913 J.A.Kraunsoe, T.D.Claridge, and G.Lowe (1996).
Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor.
  Biochemistry, 35, 9090-9096.  
8953650 J.Whisstock, A.M.Lesk, and R.Carrell (1996).
Modeling of serpin-protease complexes: antithrombin-thrombin, alpha 1-antitrypsin (358Met-->Arg)-thrombin, alpha 1-antitrypsin (358Met-->Arg)-trypsin, and antitrypsin-elastase.
  Proteins, 26, 288-303.  
8756699 K.Nordling, and I.Björk (1996).
Identification of an epitope in antithrombin appearing on insertion of the reactive-bond loop into the A beta-sheet.
  Biochemistry, 35, 10436-10440.  
8652540 M.I.Plotnick, L.Mayne, N.M.Schechter, and H.Rubin (1996).
Distortion of the active site of chymotrypsin complexed with a serpin.
  Biochemistry, 35, 7586-7590.  
8626560 P.Mikus, and T.Ny (1996).
Intracellular polymerization of the serpin plasminogen activator inhibitor type 2.
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Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor.
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  2901226 T.Nukiwa, M.L.Brantly, F.Ogushi, G.A.Fells, and R.G.Crystal (1988).
Characterization of the gene and protein of the common alpha 1-antitrypsin normal M2 allele.
  Am J Hum Genet, 43, 322-330.  
  3548750 A.Hercz (1987).
Modification of the isoinhibitors of human serum alpha 1-proteinase inhibitor (alpha 1-antitrypsin) by pancreatic proteases.
  Biol Chem Hoppe Seyler, 368, 77-84.  
3500183 F.Ogushi, G.A.Fells, R.C.Hubbard, S.D.Straus, and R.G.Crystal (1987).
Z-type alpha 1-antitrypsin is less competent than M1-type alpha 1-antitrypsin as an inhibitor of neutrophil elastase.
  J Clin Invest, 80, 1366-1374.  
2440681 H.R.Lijnen, W.E.Holmes, B.van Hoef, B.Wiman, H.Rodriguez, and D.Collen (1987).
Amino-acid sequence of human alpha 2-antiplasmin.
  Eur J Biochem, 166, 565-574.  
3499938 R.C.Foreman (1987).
Alpha 1-antitrypsin deficiency--a defect in secretion.
  Biosci Rep, 7, 307-311.  
3458172 A.E.Davis, A.S.Whitehead, R.A.Harrison, A.Dauphinais, G.A.Bruns, M.Cicardi, and F.S.Rosen (1986).
Human inhibitor of the first component of complement, C1: characterization of cDNA clones and localization of the gene to chromosome 11.
  Proc Natl Acad Sci U S A, 83, 3161-3165.  
3532120 D.J.Pickup, B.S.Ink, W.Hu, C.A.Ray, and W.K.Joklik (1986).
Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases.
  Proc Natl Acad Sci U S A, 83, 7698-7702.  
  2430793 H.Pannekoek, H.Veerman, H.Lambers, P.Diergaarde, C.L.Verweij, A.J.van Zonneveld, and J.A.van Mourik (1986).
Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family.
  EMBO J, 5, 2539-2544.  
3094014 I.L.Flink, T.J.Bailey, T.A.Gustafson, B.E.Markham, and E.Morkin (1986).
Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases.
  Proc Natl Acad Sci U S A, 83, 7708-7712.  
3486887 J.F.Mornex, A.Chytil-Weir, Y.Martinet, M.Courtney, J.P.LeCocq, and R.G.Crystal (1986).
Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals.
  J Clin Invest, 77, 1952-1961.  
3537008 R.W.Carrell (1986).
alpha 1-Antitrypsin: molecular pathology, leukocytes, and tissue damage.
  J Clin Invest, 78, 1427-1431.  
3484754 T.Nukiwa, M.Brantly, R.Garver, L.Paul, M.Courtney, J.P.LeCocq, and R.G.Crystal (1986).
Evaluation of "at risk" alpha 1-antitrypsin genotype SZ with synthetic oligonucleotide gene probes.
  J Clin Invest, 77, 528-537.  
  3640709 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.
  EMBO J, 5, 2453-2458.
PDB code: 1ppf
  3519213 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.
  EMBO J, 5, 813-818.  
3876562 D.H.Perlmutter, R.M.Kay, F.S.Cole, T.H.Rossing, D.Van Thiel, and H.R.Colten (1985).
The cellular defect in alpha 1-proteinase inhibitor (alpha 1-PI) deficiency is expressed in human monocytes and in Xenopus oocytes injected with human liver mRNA.
  Proc Natl Acad Sci U S A, 82, 6918-6921.  
3877243 R.W.Carrell, and M.C.Owen (1985).
Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis.
  Nature, 317, 730-732.  
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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