1kma: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin== | |||
<StructureSection load='1kma' size='340' side='right'caption='[[1kma]]' scene=''> | |||
| | == 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. | 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> | |||
[[Category: Dipetalogaster maximus]] | [[Category: Dipetalogaster maximus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Flemming | [[Category: Flemming J]] | ||
[[Category: Glusa | [[Category: Glusa E]] | ||
[[Category: Gorlach | [[Category: Gorlach M]] | ||
[[Category: Grosse | [[Category: Grosse F]] | ||
[[Category: Guhrs | [[Category: Guhrs K-H]] | ||
[[Category: Hartmann | [[Category: Hartmann M]] | ||
[[Category: Icke | [[Category: Icke C]] | ||
[[Category: Ohlenschlager | [[Category: Ohlenschlager O]] | ||
[[Category: Ramachandran | [[Category: Ramachandran R]] | ||
[[Category: Schlott | [[Category: Schlott B]] | ||
[[Category: Wohnert | [[Category: Wohnert J]] | ||
Latest revision as of 04:40, 17 October 2024
NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin
| ||||||||||||
