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PDBsum entry 1hle
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protein metals Protein-protein interface(s) links
Hydrolase inhibitor(serine proteinase) PDB id
1hle

 

 

 

 

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Contents
Protein chains
345 a.a. *
31 a.a. *
Metals
_CA
Waters ×636
* Residue conservation analysis
PDB id:
1hle
Name: Hydrolase inhibitor(serine proteinase)
Title: Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 angstroms resolution
Structure: Horse leukocyte elastase inhibitor. Chain: a. Engineered: yes. Horse leukocyte elastase inhibitor. Chain: b. Engineered: yes
Source: Equus caballus. Horse. Organism_taxid: 9796. Organism_taxid: 9796
Biol. unit: Tetramer (from PQS)
Resolution:
1.95Å     R-factor:   0.176    
Authors: U.Baumann,W.Bode,R.Huber,J.Travis,J.Potempa
Key ref:
U.Baumann et al. (1992). Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. J Mol Biol, 226, 1207-1218. PubMed id: 1518052 DOI: 10.1016/0022-2836(92)91062-T
Date:
13-Apr-92     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P05619  (ILEU_HORSE) -  Leukocyte elastase inhibitor from Equus caballus
Seq:
Struc: 		379 a.a.
344 a.a.*
Protein chain
P05619  (ILEU_HORSE) -  Leukocyte elastase inhibitor from Equus caballus
Seq:
Struc: 		379 a.a.
31 a.a.
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.1016/0022-2836(92)91062-T J Mol Biol 226:1207-1218 (1992)
PubMed id: 1518052  
 
 
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.
U.Baumann, W.Bode, R.Huber, J.Travis, J.Potempa.
 
  ABSTRACT  
 
The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. equence alignment according to Huber & Carrel1 (1989) of some serpis 		Figure 5.
Fig. 5.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1992, 226, 1207-1218) copyright 1992.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20940421 J.Chmelar, C.J.Oliveira, P.Rezacova, I.M.Francischetti, Z.Kovarova, G.Pejler, P.Kopacek, J.M.Ribeiro, M.Mares, J.Kopecky, and M.Kotsyfakis (2011).
A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation.
  Blood, 117, 736-744.
PDB code: 3nda
19486669 S.Yang, S.Park, L.Makowski, and B.Roux (2009).
A rapid coarse residue-based computational method for x-ray solution scattering characterization of protein folds and multiple conformational states of large protein complexes.
  Biophys J, 96, 4449-4463.  
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.  
11555638 D.N.Saunders, L.Jankova, S.J.Harrop, P.M.Curmi, A.R.Gould, M.Ranson, and M.S.Baker (2001).
Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2.
  J Biol Chem, 276, 43383-43389.  
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
  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.  
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
  10975564 M.Simonovic, Gettins PGW, and K.Volz (2000).
Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition.
  Protein Sci, 9, 1423-1427.
PDB codes: 1c8o 1m93
  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
10966577 X.Zhou, F.Alber, G.Folkers, G.H.Gonnet, and G.Chelvanayagam (2000).
An analysis of the helix-to-strand transition between peptides with identical sequence.
  Proteins, 41, 248-256.  
10026180 S.A.Grigoryev, J.Bednar, and C.L.Woodcock (1999).
MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member.
  J Biol Chem, 274, 5626-5636.  
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.  
9521649 C.M.Lukacs, H.Rubin, and D.W.Christianson (1998).
Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.
  Biochemistry, 37, 3297-3304.
PDB codes: 1as4 3caa 4caa
9538691 J.Whisstock, R.Skinner, and A.M.Lesk (1998).
An atlas of serpin conformations.
  Trends Biochem Sci, 23, 63-67.  
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.  
  9007980 W.S.Chang, J.Whisstock, P.C.Hopkins, A.M.Lesk, R.W.Carrell, and M.R.Wardell (1997).
Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins.
  Protein Sci, 6, 89-98.  
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.  
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
  8931141 H.Koloczek, A.Banbula, G.S.Salvesen, and J.Potempa (1996).
Serpin alpha 1proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy.
  Protein Sci, 5, 2226-2235.  
8787534 H.T.Wright (1996).
The structural puzzle of how serpin serine proteinase inhibitors work.
  Bioessays, 18, 453-464.  
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.  
8942989 N.Mathialagan, and T.R.Hansen (1996).
Pepsin-inhibitory activity of the uterine serpins.
  Proc Natl Acad Sci U S A, 93, 13653-13658.  
7622502 D.A.Lomas, P.R.Elliott, S.K.Sidhar, R.C.Foreman, J.T.Finch, D.W.Cox, J.C.Whisstock, and R.W.Carrell (1995).
alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.
  J Biol Chem, 270, 16864-16870.  
7890640 D.A.Lomas, P.R.Elliott, W.S.Chang, M.R.Wardell, and R.W.Carrell (1995).
Preparation and characterization of latent alpha 1-antitrypsin.
  J Biol Chem, 270, 5282-5288.  
7479695 H.T.Wright, and J.N.Scarsdale (1995).
Structural basis for serpin inhibitor activity.
  Proteins, 22, 210-225.  
8017761 P.A.Patston, P.G.Gettins, and M.Schapira (1994).
The mechanism by which serpins inhibit thrombin and other serine proteinases.
  Ann N Y Acad Sci, 714, 13-20.  
8087553 R.W.Carrell, P.E.Stein, G.Fermi, and M.R.Wardell (1994).
Biological implications of a 3 A structure of dimeric antithrombin.
  Structure, 2, 257-270.
PDB code: 1ant
7901009 W.F.Teschauer, R.Mentele, and C.P.Sommerhoff (1993).
Primary structure of a porcine leukocyte serpin.
  Eur J Biochem, 217, 519-526.  
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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