1kma

<StructureSection load='1kma' size='340' side='right' caption='[[1kma]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1kma]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood-sucking_bug Blood-sucking bug]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KMA FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kma OCA], [http://pdbe.org/1kma PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kma RCSB], [http://www.ebi.ac.uk/pdbsum/1kma PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kma ProSAT]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kma_consurf.spt"</scriptWhenChecked>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kma" style="background-color:#fffaf0;"></div>

[[Category: Blood-sucking bug]]

[[Category: Flemming, J]]

[[Category: Glusa, E]]

[[Category: Gorlach, M]]

[[Category: Grosse, F]]

[[Category: Guhrs, K H]]

[[Category: Hartmann, M]]

[[Category: Icke, C]]

[[Category: Ohlenschlager, O]]

[[Category: Ramachandran, R]]

[[Category: Schlott, B]]

[[Category: Wohnert, J]]

[[Category: Kazal-type]]