1kma
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(New page: 200px<br /><applet load="1kma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kma" /> '''NMR Structure of the Domain-I of the Kazal-t...)
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Revision as of 17:14, 20 November 2007
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NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin
Overview
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.
About this Structure
1KMA is a Single protein structure of sequence from Dipetalogaster maximus. Full crystallographic information is available from OCA.
Reference
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
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