1den
From Proteopedia
(New page: 200px<br /><applet load="1den" size="450" color="white" frame="true" align="right" spinBox="true" caption="1den" /> '''PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM...) |
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| - | [[Image:1den.gif|left|200px]]<br /><applet load="1den" size=" | + | [[Image:1den.gif|left|200px]]<br /><applet load="1den" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1den" /> | caption="1den" /> | ||
'''PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS'''<br /> | '''PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report here the NMR structure of dendrotoxin I, a powerful potassium | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DEN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http:// | + | 1DEN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dendroaspis polylepis polylepis]] | [[Category: Dendroaspis polylepis polylepis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Foray, M | + | [[Category: Foray, M F.]] |
| - | [[Category: Lancelin, J | + | [[Category: Lancelin, J M.]] |
[[Category: venom(potassium channel inhibitor)]] | [[Category: venom(potassium channel inhibitor)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:52 2008'' |
Revision as of 10:15, 21 February 2008
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PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS
Overview
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.
About this Structure
1DEN is a Single protein structure of sequence from Dendroaspis polylepis polylepis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:15:52 2008
