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1kma

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[[Image:1kma.gif|left|200px]]
 
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{{Structure
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==NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin==
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|PDB= 1kma |SIZE=350|CAPTION= <scene name='initialview01'>1kma</scene>
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<StructureSection load='1kma' size='340' side='right'caption='[[1kma]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1kma]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMA FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kma OCA], [https://pdbe.org/1kma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kma RCSB], [https://www.ebi.ac.uk/pdbsum/1kma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kma ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin'''
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[https://www.uniprot.org/uniprot/DPGN_DIPMA DPGN_DIPMA] Thrombin inhibitor. Prevents blood clotting to allow insect to feed on blood. Also functions as an inhibitor of trypsin and plasmin.<ref>PMID:10702701</ref> <ref>PMID:10561601</ref> <ref>PMID:12051857</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kma_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kma ConSurf].
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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]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Dipetalogaster maximus]]
[[Category: Dipetalogaster maximus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Flemming, J.]]
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[[Category: Flemming J]]
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[[Category: Glusa, E.]]
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[[Category: Glusa E]]
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[[Category: Gorlach, M.]]
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[[Category: Gorlach M]]
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[[Category: Grosse, F.]]
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[[Category: Grosse F]]
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[[Category: Guhrs, K H.]]
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[[Category: Guhrs K-H]]
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[[Category: Hartmann, M.]]
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[[Category: Hartmann M]]
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[[Category: Icke, C.]]
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[[Category: Icke C]]
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[[Category: Ohlenschlager, O.]]
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[[Category: Ohlenschlager O]]
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[[Category: Ramachandran, R.]]
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[[Category: Ramachandran R]]
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[[Category: Schlott, B.]]
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[[Category: Schlott B]]
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[[Category: Wohnert, J.]]
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[[Category: Wohnert J]]
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[[Category: disulphide-rich small alpha+beta fold]]
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[[Category: kazal-type]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:18 2008''
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Current revision

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

PDB ID 1kma

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