1kma
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1kma.png|left|200px]] | ||
| - | + | ==NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin== | |
| - | + | <StructureSection load='1kma' size='340' side='right'caption='[[1kma]]' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |
| - | -- | + | <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> |
| - | + | </table> | |
| + | == Function == | ||
| + | [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> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kma_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:12051857</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1kma" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
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| - | == | + | |
| - | < | + | |
[[Category: Dipetalogaster maximus]] | [[Category: Dipetalogaster maximus]] | ||
| - | [[Category: Flemming | + | [[Category: Large Structures]] |
| - | [[Category: Glusa | + | [[Category: Flemming J]] |
| - | [[Category: Gorlach | + | [[Category: Glusa E]] |
| - | [[Category: Grosse | + | [[Category: Gorlach M]] |
| - | [[Category: Guhrs | + | [[Category: Grosse F]] |
| - | [[Category: Hartmann | + | [[Category: Guhrs K-H]] |
| - | [[Category: Icke | + | [[Category: Hartmann M]] |
| - | [[Category: Ohlenschlager | + | [[Category: Icke C]] |
| - | [[Category: Ramachandran | + | [[Category: Ohlenschlager O]] |
| - | [[Category: Schlott | + | [[Category: Ramachandran R]] |
| - | [[Category: Wohnert | + | [[Category: Schlott B]] |
| - | + | [[Category: Wohnert J]] | |
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Current revision
NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin
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