Proteopedia

1kma

NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor DipetalinNMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin

Structural highlights

1kma is a 1 chain structure with sequence from Dipetalogaster maximus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPGN_DIPMA Thrombin inhibitor. Prevents blood clotting to allow insect to feed on blood. Also functions as an inhibitor of trypsin and plasmin.[1] [2] [3]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The interaction of domains of the Kazal-type inhibitor protein dipetalin with the serine proteinases thrombin and trypsin is studied. The functional studies of the recombinantly expressed domains (Dip-I+II, Dip-I and Dip-II) allow the dissection of the thrombin inhibitory properties and the identification of Dip-I as a key contributor to thrombin/dipetalin complex stability and its inhibitory potency. Furthermore, Dip-I, but not Dip-II, forms a complex with trypsin resulting in an inhibition of the trypsin activity directed towards protein substrates. The high resolution NMR structure of the Dip-I domain is determined using multi-dimensional heteronuclear NMR spectroscopy. Dip-I exhibits the canonical Kazal-type fold with a central alpha-helix and a short two-stranded antiparallel beta-sheet. Molecular regions essential for inhibitor complex formation with thrombin and trypsin are identified. A comparison with molecular complexes of other Kazal-type thrombin and trypsin inhibitors by molecular modeling shows that the N-terminal segment of Dip-I fulfills the structural prerequisites for inhibitory interactions with either proteinase and explains the capacity of this single Kazal-type domain to interact with different proteinases.

Interaction of Kazal-type inhibitor domains with serine proteinases: biochemical and structural studies.,Schlott B, Wohnert J, Icke C, Hartmann M, Ramachandran R, Guhrs KH, Glusa E, Flemming J, Gorlach M, Grosse F, Ohlenschlager O J Mol Biol. 2002 Apr 26;318(2):533-46. PMID:12051857[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Lange U, Keilholz W, Schaub GA, Landmann H, Markwardt F, Nowak G. Biochemical characterization of a thrombin inhibitor from the bloodsucking bug Dipetalogaster maximus. Haemostasis. 1999;29(4):204-11. PMID:10702701
  2. ↑ Mende K, Petoukhova O, Koulitchkova V, Schaub GA, Lange U, Kaufmann R, Nowak G. Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization. Eur J Biochem. 1999 Dec;266(2):583-90. PMID:10561601
  3. ↑ Schlott B, Wohnert J, Icke C, Hartmann M, Ramachandran R, Guhrs KH, Glusa E, Flemming J, Gorlach M, Grosse F, Ohlenschlager O. Interaction of Kazal-type inhibitor domains with serine proteinases: biochemical and structural studies. J Mol Biol. 2002 Apr 26;318(2):533-46. PMID:12051857 doi:10.1016/S0022-2836(02)00014-1
  4. ↑ Schlott B, Wohnert J, Icke C, Hartmann M, Ramachandran R, Guhrs KH, Glusa E, Flemming J, Gorlach M, Grosse F, Ohlenschlager O. Interaction of Kazal-type inhibitor domains with serine proteinases: biochemical and structural studies. J Mol Biol. 2002 Apr 26;318(2):533-46. PMID:12051857 doi:10.1016/S0022-2836(02)00014-1
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