1apf
From Proteopedia
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| - | [[Image:1apf.gif|left|200px]] | + | [[Image:1apf.gif|left|200px]] |
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| - | '''ANTHOPLEURIN-B, NMR, 20 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1apf |SIZE=350|CAPTION= <scene name='initialview01'>1apf</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''ANTHOPLEURIN-B, NMR, 20 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1APF is a [ | + | 1APF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anthopleura_xanthogrammica Anthopleura xanthogrammica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APF OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7582896 7582896] |
[[Category: Anthopleura xanthogrammica]] | [[Category: Anthopleura xanthogrammica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:38 2008'' |
Revision as of 08:00, 20 March 2008
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ANTHOPLEURIN-B, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1APF is a Single protein structure of sequence from Anthopleura xanthogrammica. Full crystallographic information is available from OCA.
Reference
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
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