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1kma
From Proteopedia
(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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| - | [[Image:1kma.gif|left|200px]]<br /><applet load="1kma" size=" | + | [[Image:1kma.gif|left|200px]]<br /><applet load="1kma" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin'''<br /> | '''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The interaction of domains of the Kazal-type inhibitor protein dipetalin | + | 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== | ==About this Structure== | ||
| - | 1KMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dipetalogaster_maximus Dipetalogaster maximus]. Full crystallographic information is available from [http:// | + | 1KMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dipetalogaster_maximus Dipetalogaster maximus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gorlach, M.]] | [[Category: Gorlach, M.]] | ||
[[Category: Grosse, F.]] | [[Category: Grosse, F.]] | ||
| - | [[Category: Guhrs, K | + | [[Category: Guhrs, K H.]] |
[[Category: Hartmann, M.]] | [[Category: Hartmann, M.]] | ||
[[Category: Icke, C.]] | [[Category: Icke, C.]] | ||
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[[Category: kazal-type]] | [[Category: kazal-type]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:39 2008'' |
Revision as of 11:35, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:35:39 2008
