1pnh: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1pnh.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1pnh", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1pnh|  PDB=1pnh  |  SCENE=  }}
'''SOLUTION STRUCTURE OF PO5-NH2, A SCORPION TOXIN ANALOG WITH HIGH AFFINITY FOR THE APAMIN-SENSITIVE POTASSIUM CHANNEL'''


==SOLUTION STRUCTURE OF PO5-NH2, A SCORPION TOXIN ANALOG WITH HIGH AFFINITY FOR THE APAMIN-SENSITIVE POTASSIUM CHANNEL==
<StructureSection load='1pnh' size='340' side='right'caption='[[1pnh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pnh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_mauritanicus_mauritanicus Androctonus mauritanicus mauritanicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PNH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</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=1pnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pnh OCA], [https://pdbe.org/1pnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pnh RCSB], [https://www.ebi.ac.uk/pdbsum/1pnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pnh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAX52_ANDMA KAX52_ANDMA] Blocker for the small conductance calcium-activated potassium channels (SK-Ca); also known as apamine-sensitive potassium channel.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The venom of the scorpion Androctonus mauretanicus mauretanicus contains a toxin--P05--which is structurally and functionally similar to scorpion leiurotoxin I (87% sequence identity), a blocker of the apamin-sensitive Ca(2+)-activated K+ channels. P05, a 31-residue polypeptide cross-linked by three disulfide bridges, also possesses binding and physiological properties similar to those of the bee venom toxin apamin (18 residues, two disulfides). However, the amino acid sequences of these two polypeptides are dissimilar, except for a common Arg-Arg-Cys-Gln motif which is located on an alpha-helix. P05-NH2, a synthetic analog of P05, unlike native P05, was found to bind irreversibly to the apamin receptor. The solution structure of P05-NH2 has been solved by conventional two-dimensional NMR techniques followed by distance geometry and energy minimization. The obtained conformation is composed of two and an half turns of alpha-helix (residues 5-14) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 17-22 and 25-29). This beta-sheet has a right-handed twist as usual for such secondary structures. The beta-turn connecting the two strands belongs to type II'. This structure is homologous to all scorpion toxin structures known so far as well as to insect defensins. The three arginines known to be involved in the pharmacological activity, i.e., Arg6, Arg7, and Arg13, are all located on the solvent-exposed side of the helix and form a positively charged surface which includes Gln9. The calculated electrostatic potential is highly asymmetric with the greatest positive potential centered on the Arg-rich alpha-helix side.(ABSTRACT TRUNCATED AT 250 WORDS)


==Overview==
Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel.,Meunier S, Bernassau JM, Sabatier JM, Martin-Eauclaire MF, Van Rietschoten J, Cambillau C, Darbon H Biochemistry. 1993 Nov 16;32(45):11969-76. PMID:8218272<ref>PMID:8218272</ref>
The venom of the scorpion Androctonus mauretanicus mauretanicus contains a toxin--P05--which is structurally and functionally similar to scorpion leiurotoxin I (87% sequence identity), a blocker of the apamin-sensitive Ca(2+)-activated K+ channels. P05, a 31-residue polypeptide cross-linked by three disulfide bridges, also possesses binding and physiological properties similar to those of the bee venom toxin apamin (18 residues, two disulfides). However, the amino acid sequences of these two polypeptides are dissimilar, except for a common Arg-Arg-Cys-Gln motif which is located on an alpha-helix. P05-NH2, a synthetic analog of P05, unlike native P05, was found to bind irreversibly to the apamin receptor. The solution structure of P05-NH2 has been solved by conventional two-dimensional NMR techniques followed by distance geometry and energy minimization. The obtained conformation is composed of two and an half turns of alpha-helix (residues 5-14) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 17-22 and 25-29). This beta-sheet has a right-handed twist as usual for such secondary structures. The beta-turn connecting the two strands belongs to type II'. This structure is homologous to all scorpion toxin structures known so far as well as to insect defensins. The three arginines known to be involved in the pharmacological activity, i.e., Arg6, Arg7, and Arg13, are all located on the solvent-exposed side of the helix and form a positively charged surface which includes Gln9. The calculated electrostatic potential is highly asymmetric with the greatest positive potential centered on the Arg-rich alpha-helix side.(ABSTRACT TRUNCATED AT 250 WORDS)


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PNH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_mauretanicus_mauretanicus Androctonus mauretanicus mauretanicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNH OCA].
</div>
<div class="pdbe-citations 1pnh" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel., Meunier S, Bernassau JM, Sabatier JM, Martin-Eauclaire MF, Van Rietschoten J, Cambillau C, Darbon H, Biochemistry. 1993 Nov 16;32(45):11969-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8218272 8218272]
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
[[Category: Androctonus mauretanicus mauretanicus]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Bernassau, J M.]]
__TOC__
[[Category: Cambillau, C.]]
</StructureSection>
[[Category: Darbon, H.]]
[[Category: Androctonus mauritanicus mauritanicus]]
[[Category: Martin-Eauclaire, M F.]]
[[Category: Large Structures]]
[[Category: Meunier, S.]]
[[Category: Bernassau J-M]]
[[Category: Rietschoten, J Van.]]
[[Category: Cambillau C]]
[[Category: Sabatier, J M.]]
[[Category: Darbon H]]
[[Category: Toxin]]
[[Category: Martin-Eauclaire M-F]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:16:49 2008''
[[Category: Meunier S]]
[[Category: Sabatier J-M]]
[[Category: Van Rietschoten J]]
Retrieved from "https://proteopedia.org/1pnh"