1dtk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dtk]] is a 1 chain structure with sequence from [http://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=1DTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DTK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dtk]] is a 1 chain structure with sequence from [http://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=1DTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DTK FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dtk RCSB], [http://www.ebi.ac.uk/pdbsum/1dtk PDBsum]</span></td></tr> | </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=1dtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dtk RCSB], [http://www.ebi.ac.uk/pdbsum/1dtk PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dendroaspis polylepis polylepis]] | [[Category: Dendroaspis polylepis polylepis]] | ||
[[Category: Berndt, K | [[Category: Berndt, K]] | ||
[[Category: Guntert, P | [[Category: Guntert, P]] | ||
[[Category: Wuthrich, K | [[Category: Wuthrich, K]] | ||
[[Category: Presynaptic neurotoxin]] | [[Category: Presynaptic neurotoxin]] | ||
Revision as of 00:37, 23 December 2014
THE NMR SOLUTION STRUCTURE OF DENDROTOXIN K FROM THE VENOM OF DENDROASPIS POLYLEPIS POLYLEPISTHE NMR SOLUTION STRUCTURE OF DENDROTOXIN K FROM THE VENOM OF DENDROASPIS POLYLEPIS POLYLEPIS
Structural highlights
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 PubMedThe solution structure of dendrotoxin K (Toxin K), a protein consisting of one polypeptide chain with 57 residues purified from the venom of the black mamba, Dendroaspis polylepis polylepis, was determined by nuclear magnetic resonance (NMR) spectroscopy. On the basis of virtually complete sequence-specific 1H NMR assignments, including individual assignments for 38 pairs of diastereotopic substituents and side-chain amide protons, a total of 818 nuclear Overhauser effect distance constraints and 123 dihedral angle constraints were identified. Using this input, the solution structure of Toxin K was calculated with the program DIANA, and refined by restrained energy-minimization with a modified version of the program AMBER. The average root-mean-square deviation (r.m.s.d.) relative to the mean atomic co-ordinates of the 20 conformers selected to represent the solution structure is 0.31 A for all backbone atoms N, C alpha and C', and 0.90 A for all heavy-atoms of residues 2 to 56. The solution structure of Toxin K is very similar to the solution structure of the basic pancreatic trypsin inhibitor (BPTI) and the X-ray crystal structure of the alpha-dendrotoxin from Dendroaspis angusticeps (alpha-DTX), with r.m.s.d. values of 1.31 A and 0.92 A, respectively, for the backbone atoms of residues 2 to 56. Some local structural differences between Toxin K and BPTI are directly related to the fact that intermolecular interactions with two of the four internal molecules of hydration water in BPTI are replaced by intramolecular hydrogen bonds in Toxin K. Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis.,Berndt KD, Guntert P, Wuthrich K J Mol Biol. 1993 Dec 5;234(3):735-50. PMID:8254670[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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