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1apf

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Revision as of 03:18, 10 September 2015

ANTHOPLEURIN-B, NMR, 20 STRUCTURES

Structural highlights

1apf is a 1 chain structure with sequence from Anthopleura xanthogrammica. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TXAB_ANTXA] Binds specifically to the sodium channel (site 3) (Nav), thereby delaying its inactivation during signal transduction. Thus it strongly stimulates mammalian cardiac muscle contraction. Does not display phospholipid-binding activity. Anthopleurin-B is the most potent peptide heart stimulator isolated from the sea anemone.

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

BACKGROUND: The polypeptide anthopleurin-B (AP-B) is one of a number of related toxins produced by sea anemones. AP-B delays inactivation of the voltage-gated sodium channel of excitable tissue. In the mammalian heart, this effect is manifest as an increase in the force of contraction. As a result, there is interest in exploiting the anthopleurins as lead compounds in the design of novel cardiac stimulants. Essential to this endeavour is a high-resolution solution structure of the molecule describing the positions of functionally important side chains. RESULTS: AP-B exists in multiple conformations in solution as a result of cis-trans isomerization about the Gly40-Pro41 peptide bond. The solution structure of the major conformer of AP-B has been determined by two-dimensional 1H NMR at pH 4.5 and 25 degrees C. The core structure is a four-stranded, antiparallel beta-sheet (residues 2-4, 20-23, 34-37 and 45-48) and includes several beta-turns (6-9, 25-28, 30-33). Three loops connect the beta-strands, the longest and least well defined being the first loop, extending from residues 8-17. These features are shared by other members of this family of sea anemone toxins. The locations of a number of side chains which are important for the cardiac stimulatory activity of AP-B are well defined in the structures. CONCLUSIONS: We have described the solution structure of AP-B and compared it with that of AP-A, from which it differs by substitutions at seven amino acid positions. It shares an essentially identical fold with AP-A yet is about 10-fold more active. Comparison of the structures, particularly in the region of residues essential for activity, gives a clearer indication of the location and extent of the cardioactive pharmacophore in these polypeptides.

Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A.,Monks SA, Pallaghy PK, Scanlon MJ, Norton RS Structure. 1995 Aug 15;3(8):791-803. PMID:7582896^[1]

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

References

↑ Monks SA, Pallaghy PK, Scanlon MJ, Norton RS. Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A. Structure. 1995 Aug 15;3(8):791-803. PMID:7582896

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1apf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anthopleura_xanthogrammica Anthopleura xanthogrammica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APF FirstGlance]. <br>
-</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=1apf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1apf RCSB], [http://www.ebi.ac.uk/pdbsum/1apf 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=1apf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apf OCA], [http://pdbe.org/1apf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apf RCSB], [http://www.ebi.ac.uk/pdbsum/1apf PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1apf" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1apf

From Proteopedia

Revision as of 03:18, 10 September 2015

ANTHOPLEURIN-B, NMR, 20 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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