2YYF
Purification and structural characterization of a D-amino acid containing conopeptide, marmophine, from Conus marmoreus
Summary for 2YYF
| Entry DOI | 10.2210/pdb2yyf/pdb |
| Related | 1E75 1FU3 1JLP 1QS3 |
| NMR Information | BMRB: 7397 |
| Descriptor | M-conotoxin mr12 (1 entity in total) |
| Functional Keywords | m-conotoxin mr12, mr1931, toxin |
| Total number of polymer chains | 1 |
| Total formula weight | 1934.05 |
| Authors | |
| Primary citation | Han, Y.,Huang, F.,Jiang, H.,Liu, L.,Wang, Q.,Wang, Y.,Shao, X.,Chi, C.,Du, W.,Wang, C. Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus. Febs J., 275:1976-1987, 2008 Cited by PubMed Abstract: Cone snails, a group of gastropod animals that inhabit tropical seas, are capable of producing a mixture of peptide neurotoxins, namely conotoxins, for defense and predation. Conotoxins are mainly disulfide-rich short peptides that act on different ion channels, neurotransmitter receptors, or transporters in the nervous system. They exhibit highly diverse compositions, structures, and biological functions. In this work, a novel Cys-free 15-residue conopeptide from Conus marmoreus was purified and designated as conomarphin. Conomarphin is unique because of its D-configuration Phe at the third residue from the C-terminus, which was identified using HPLC by comparing native conomarphin fragments and the corresponding synthetic peptides cleaved by different proteases. Surprisingly, the cDNA-encoded precursor of conomarphin was found to share the conserved signal peptide with other M-superfamily conotoxins, clearly indicating that conomarphin should belong to the M-superfamily, although conomarphin shares no homology with other six-Cys-containing M-superfamily conotoxins. Furthermore, NMR spectroscopy experiments established that conomarphin adopts a well-defined structure in solution, with a tight loop in the middle of the peptide and a short 3(10)-helix at the C-terminus. By contrast, no loop in L-Phe13-conomarphin was found, which suggests that D-Phe13 is essential for the structure of conomarphin. In conclusion, conomarphin may represent a new conotoxin family, whose biological activity remains to be identified. PubMed: 18355315DOI: 10.1111/j.1742-4658.2008.06352.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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