1dem
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEM FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEM FirstGlance]. <br> | ||
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1dem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dem OCA], [https://pdbe.org/1dem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dem RCSB], [https://www.ebi.ac.uk/pdbsum/1dem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dem ProSAT]</span></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=1dem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dem OCA], [https://pdbe.org/1dem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dem RCSB], [https://www.ebi.ac.uk/pdbsum/1dem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dem ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1dem_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1dem_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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=1dem ConSurf]. | </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=1dem ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report here the NMR structure of dendrotoxin I, a powerful potassium channel blocker from the venom of the African Elapidae snake Dendroaspis polylepis polylepis (black mamba), calculated from an experimentally-derived set of 719 geometric restraints. The backbone of the toxin superimposes on bovine pancreatic trypsin inhibitor (BPTI) with a root-mean-square deviation of < 1.7 A. The surface electrostatic potential calculated for dendrotoxin I and BPTI, reveal an important difference which might account for the differences in function of the two proteins. These proteins may provide examples of adaptation for specific and diverse biological functions while at the same time maintaining the overall three-dimensional structure of a common ancestor. | ||
| + | |||
| + | Proteinase inhibitor homologues as potassium channel blockers.,Lancelin JM, Foray MF, Poncin M, Hollecker M, Marion D Nat Struct Biol. 1994 Apr;1(4):246-50. PMID:7544683<ref>PMID:7544683</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1dem" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS
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