1KMA
NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin
Summary for 1KMA
| Entry DOI | 10.2210/pdb1kma/pdb |
| NMR Information | BMRB: 5276 |
| Descriptor | DIPETALIN (1 entity in total) |
| Functional Keywords | disulphide-rich small alpha+beta fold, kazal-type, blood clotting |
| Biological source | Dipetalogaster maximus |
| Cellular location | Secreted: O96790 |
| Total number of polymer chains | 1 |
| Total formula weight | 6090.67 |
| Authors | Schlott, B.,Wohnert, J.,Icke, C.,Hartmann, M.,Ramachandran, R.,Guhrs, K.-H.,Glusa, E.,Flemming, J.,Gorlach, M.,Grosse, F.,Ohlenschlager, O. (deposition date: 2001-12-14, release date: 2002-05-15, Last modification date: 2024-10-16) |
| Primary citation | Schlott, B.,Wohnert, J.,Icke, C.,Hartmann, M.,Ramachandran, R.,Guhrs, K.H.,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., 318:533-546, 2002 Cited by PubMed Abstract: 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. PubMed: 12051857DOI: 10.1016/S0022-2836(02)00014-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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