1kma: Difference between revisions

Revision as of 10:32, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kma.png

Template:STRUCTURE 1kma

NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor DipetalinNMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin

Template:ABSTRACT PUBMED 12051857

About this StructureAbout this Structure

1KMA is a Single protein structure of sequence from Dipetalogaster maximus. Full experimental information is available from OCA.

ReferenceReference

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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OCA

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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===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12051857}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12051857}}
 ==About this Structure==
-KMA 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].
+KMA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dipetalogaster_maximus Dipetalogaster maximus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMA OCA].
 ==Reference==
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 [[Category: Disulphide-rich small alpha+beta fold]]
 [[Category: Kazal-type]]
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