1kma
From Proteopedia
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| - | [[Image:1kma.gif|left|200px]] | + | [[Image:1kma.gif|left|200px]] |
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| - | '''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin''' | + | {{Structure |
| + | |PDB= 1kma |SIZE=350|CAPTION= <scene name='initialview01'>1kma</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KMA is a [ | + | 1KMA is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12051857 12051857] |
[[Category: Dipetalogaster maximus]] | [[Category: Dipetalogaster maximus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: kazal-type]] | [[Category: kazal-type]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:18 2008'' |
Revision as of 10:19, 20 March 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 Mar 20 12:19:18 2008
