1dtx

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<StructureSection load='1dtx' size='340' side='right'caption='[[1dtx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1dtx' size='340' side='right'caption='[[1dtx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1dtx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bmnh_1946.1.20.48 Bmnh 1946.1.20.48]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1dtx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1dtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtx OCA], [https://pdbe.org/1dtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dtx RCSB], [https://www.ebi.ac.uk/pdbsum/1dtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dtx 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=1dtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtx OCA], [https://pdbe.org/1dtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dtx RCSB], [https://www.ebi.ac.uk/pdbsum/1dtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dtx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/VKTHA_DENAN VKTHA_DENAN]] Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC(50)=0.4-150 nM) and facilitates neurotransmitter release.<ref>PMID:10936620</ref> <ref>PMID:23771044</ref>
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[https://www.uniprot.org/uniprot/VKTHA_DENAN VKTHA_DENAN] Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC(50)=0.4-150 nM) and facilitates neurotransmitter release.<ref>PMID:10936620</ref> <ref>PMID:23771044</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1dtx 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=1dtx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The three-dimensional structure of alpha-dendrotoxin (alpha-DTX) from the green mamba (Dendroaspis angusticeps) venom has been determined crystallographically using the method of isomorphous replacement and refined at 2.2 A resolution using a restrained least-squares method. The crystallographic R-factor is 0.169 for all 3451 measured reflections between 7.0 and 2.2 A. Although the main-chain fold of alpha-DTX is similar to that of homologous bovine pancreatic trypsin inhibitor (BPTI), there are significant differences involving segments of the polypeptide chain close to the "antiprotease site" of BPTI. Comparison of the structure of alpha-DTX with the existing models of BPTI and its complexes with trypsin and kallikrein reveals structural differences that explain the inability of alpha-DTX to inhibit trypsin and chymotrypsin.
 
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Crystal structure of alpha-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor.,Skarzynski T J Mol Biol. 1992 Apr 5;224(3):671-83. PMID:1373774<ref>PMID:1373774</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1dtx" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bmnh 1946 1.20 48]]
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[[Category: Dendroaspis angusticeps]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Skarzynski, T]]
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[[Category: Skarzynski T]]
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[[Category: Presynaptic neurotoxin]]
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Revision as of 09:53, 20 March 2024

CRYSTAL STRUCTURE OF ALPHA-DENDROTOXIN FROM THE GREEN MAMBA VENOM AND ITS COMPARISON WITH THE STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR

PDB ID 1dtx

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