1kma

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[[Image:1kma.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kma OCA], [http://www.ebi.ac.uk/pdbsum/1kma PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kma RCSB]</span>
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'''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin'''
'''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin'''
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[[Category: Schlott, B.]]
[[Category: Schlott, B.]]
[[Category: Wohnert, J.]]
[[Category: Wohnert, J.]]
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[[Category: disulphide-rich small alpha+beta fold]]
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[[Category: Disulphide-rich small alpha+beta fold]]
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[[Category: kazal-type]]
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[[Category: Kazal-type]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:31 2008''
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Revision as of 19:54, 2 May 2008

Template:STRUCTURE 1kma

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 Page seeded by OCA on Fri May 2 22:54:35 2008

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