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PDBsum entry 1tap
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Proteinase inhibitor PDB id
1tap

 

 

 

 

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Contents
Protein chain
60 a.a.
PDB id:
1tap
Name: Proteinase inhibitor
Title: Nmr solution structure of recombinant tick anticoagulant protein (rtap), a factor xa inhibitor from the tick ornithodoros moubata
Structure: Factor xa inhibitor. Chain: a. Engineered: yes
Source: Ornithodoros moubata. Organism_taxid: 6938
NMR struc: 20 models
Authors: W.Antuch,P.Guntert,M.Billeter,K.Wuthrich
Key ref: W.Antuch et al. (1994). NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata. FEBS Lett, 352, 251-257. PubMed id: 7925983 DOI: 10.1016/0014-5793(94)00941-4
Date:
16-Aug-94     Release date:   30-Nov-94    
PROCHECK
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 Headers
 References

Protein chain
P17726  (TAP_ORNMO) -  Tick anticoagulant peptide from Ornithodoros moubata
Seq:
Struc: 		60 a.a.
60 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1016/0014-5793(94)00941-4 FEBS Lett 352:251-257 (1994)
PubMed id: 7925983  
 
 
NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata.
W.Antuch, P.Güntert, M.Billeter, T.Hawthorne, H.Grossenbacher, K.Wüthrich.
 
  ABSTRACT  
 
The solution structure of the recombinant tick anticoagulant protein (rTAP) was determined by 1H nuclear magnetic resonance (NMR) spectroscopy in aqueous solution at pH 3.6 and 36 degrees C. rTAP is a 60-residue protein functioning as a highly specific inhibitor of the coagulation protease factor Xa, which was originally isolated from the tick Ornithodoros moubata. Its regular secondary structure consists of a two-stranded antiparallel beta-sheet with residues 22-28 and 32-38, and an alpha-helix with residues 51-60. The relative orientation of these regular secondary structure elements has nearly identical counterparts in the bovine pancreatic trypsin inhibitor (BPTI). In contrast, the loop between the beta-sheet and the C-terminal alpha-helix as well as the N-terminal 20-residue segment preceding the beta-sheet adopt different three-dimensional folds in the two proteins. These observations are discussed with regard to the implication of different mechanisms of protease inhibition by rTAP and by Kunitz-type protein proteinase inhibitors.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20812859 J.L.Arolas, and S.Ventura (2011).
Protease inhibitors as models for the study of oxidative folding.
  Antioxid Redox Signal, 14, 97.  
20831444 J.Y.Chang (2011).
Distinct folding pathways of two homologous disulfide proteins: bovine pancreatic trypsin inhibitor and tick anticoagulant peptide.
  Antioxid Redox Signal, 14, 127-135.  
16710754 S.Salamanca, and J.Y.Chang (2006).
Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or hirudin model.
  Protein J, 25, 275-287.  
15585533 E.Zhao, H.L.Liu, C.H.Tsai, H.K.Tsai, C.H.Chan, and C.Y.Kao (2005).
Cysteine separations profiles on protein sequences infer disulfide connectivity.
  Bioinformatics, 21, 1415-1420.  
12945044 C.C.Chuang, C.Y.Chen, J.M.Yang, P.C.Lyu, and J.K.Hwang (2003).
Relationship between protein structures and disulfide-bonding patterns.
  Proteins, 53, 1-5.  
11932256 B.J.Mans, A.I.Louw, and A.W.Neitz (2002).
Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold.
  J Biol Chem, 277, 21371-21378.  
12172443 K.A.Bauer, B.I.Eriksson, M.R.Lassen, and A.G.Turpie (2002).
Factor Xa inhibition in the prevention of venous thromboembolism and treatment of patients with venous thromboembolism.
  Curr Opin Pulm Med, 8, 398-404.  
  10716178 R.St Charles, K.Padmanabhan, R.V.Arni, K.P.Padmanabhan, and A.Tulinsky (2000).
Structure of tick anticoagulant peptide at 1.6 A resolution complexed with bovine pancreatic trypsin inhibitor.
  Protein Sci, 9, 265-272.
PDB code: 1d0d
10089317 A.Wei, A.Smallwood, R.S.Alexander, J.Duke, H.Ross, S.A.Rosenfeld, and C.H.Chang (1999).
Crystallization and preliminary X-ray diffraction data of the complex of recombinant tick anticoagulant peptide (rTAP) and bovine factor Xa.
  Acta Crystallogr D Biol Crystallogr, 55, 862-864.  
9867819 J.Y.Chang (1999).
Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers.
  J Biol Chem, 274, 123-128.  
  8880922 A.T.Alexandrescu, S.A.Dames, and R.Wiltscheck (1996).
A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for "molten globules".
  Protein Sci, 5, 1942-1946.  
  8947023 A.van de Locht, M.T.Stubbs, W.Bode, T.Friedrich, C.Bollschweiler, W.Höffken, and R.Huber (1996).
The ornithodorin-thrombin crystal structure, a key to the TAP enigma?
  EMBO J, 15, 6011-6017.
PDB code: 1toc
  7538849 M.S.Lim-Wilby, K.Hallenga, M.de Maeyer, I.Lasters, G.P.Vlasuk, and T.K.Brunck (1995).
NMR structure determination of tick anticoagulant peptide (TAP).
  Protein Sci, 4, 178-186.
PDB code: 1tcp
7712286 M.T.Stubbs, and W.Bode (1994).
Coagulation factors and their inhibitors.
  Curr Opin Struct Biol, 4, 823-832.  
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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