1dtx

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

1dtx is a 1 chain structure with sequence from Dendroaspis angusticeps. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Harvey AL. Twenty years of dendrotoxins. Toxicon. 2001 Jan;39(1):15-26. PMID:10936620
↑ Mourao CB, Schwartz EF. Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals. Mar Drugs. 2013 Jun 14;11(6):2069-112. doi: 10.3390/md11062069. PMID:23771044 doi:http://dx.doi.org/10.3390/md11062069
↑ Skarzynski T. Crystal structure of alpha-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 5;224(3):671-83. PMID:1373774

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dtx"

Categories: Dendroaspis angusticeps | Large Structures | Skarzynski T

@@ Line 1: / Line 1: @@
-[[Image:1dtx.gif|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF ALPHA-DENDROTOXIN FROM THE GREEN MAMBA VENOM AND ITS COMPARISON WITH THE STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR==
-The line below this paragraph, containing "STRUCTURE_1dtx", creates the "Structure Box" on the page.
+<StructureSection load='1dtx' size='340' side='right'caption='[[1dtx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<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>
-{{STRUCTURE_1dtx|  PDB=1dtx  |  SCENE=  }}
+<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>
+== Function ==
+[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 ==
+[[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/dt/1dtx_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=1dtx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''CRYSTAL STRUCTURE OF ALPHA-DENDROTOXIN FROM THE GREEN MAMBA VENOM AND ITS COMPARISON WITH THE STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR'''
+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>
-==Overview==
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-DTX is a [[Single protein]] structure of sequence from [http://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].
+</div>
+<div class="pdbe-citations 1dtx" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/1373774 1373774]
+*[[Dendrotoxin|Dendrotoxin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Dendroaspis angusticeps]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Skarzynski, T.]]
+[[Category: Skarzynski T]]
-[[Category: Presynaptic neurotoxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:16:15 2008''

1dtx

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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