H
IPR011061

Hirudin/antistatin

InterPro entry
Short nameHirudin/antistatin
Overlapping entries
 
Haemadin (IPR015150)

Description

Leeches, such as Hirudo medicinalis (Medicinal leech), produce a variety of antihaemostatic proteins that act as proteinase inhibitors. These inhibitors are used to aid the leech in feeding upon its host by blocking blood coagulation
[1, 2]
. Examples of these proteins include hirustasin (inhibitor of tissue kallikrein, trypsin, alpha-chymotrypsin, and granulocyte cathepsin G)
[3]
, bdellastasin (inhibitor of trypsin, plasmin, and acrosin)
[4]
, factor Xa inhibitor antistasin (inhibitor of blood coagulation factor Xa)
[5]
, hirudin (thrombin inhibitor), decorsin (inhibitor of platelet aggregation)
[6]
and haemadin (thrombin inhibitor)
[7]
.

References

1.Proteinase inhibitors from the medicinal leech Hirudo medicinalis. Baskova IP, Zavalova LL. Biochemistry Mosc. 66, 703-14, (2001). View articlePMID: 11563948

2.Anticoagulants and inhibitors of platelet aggregation derived from leeches. Salzet M. FEBS Lett. 492, 187-92, (2001). View articlePMID: 11257492

3.The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors. Uson I, Sheldrick GM, de La Fortelle E, Bricogne G, Di Marco S, Priestle JP, Grutter MG, Mittl PR. Structure 7, 55-63, (1999). View articlePMID: 10368273

4.Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system. Rester U, Bode W, Moser M, Parry MA, Huber R, Auerswald E. J. Mol. Biol. 293, 93-106, (1999). View articlePMID: 10512718

5.X-ray structure of antistasin at 1.9 A resolution and its modelled complex with blood coagulation factor Xa. Lapatto R, Krengel U, Schreuder HA, Arkema A, de Boer B, Kalk KH, Hol WG, Grootenhuis PD, Mulders JW, Dijkema R, Theunissen HJ, Dijkstra BW. EMBO J. 16, 5151-61, (1997). View articlePMID: 9311976

6.A comparison of the effect of decorsin and two disintegrins, albolabrin and eristostatin, on platelet function. McLane MA, Gabbeta J, Rao AK, Beviglia L, Lazarus RA, Niewiarowski S. Thromb. Haemost. 74, 1316-22, (1995). PMID: 8607116

7.Characterization of the residues involved in the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. Richardson JL, Fuentes-Prior P, Sadler JE, Huber R, Bode W. Biochemistry 41, 2535-42, (2002). View articlePMID: 11851400

GO terms

biological process

  • None

cellular component

  • None
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