2N24

Solution NMR structure of Contryphan-Vc1

Summary for 2N24

• Entry DOI: 10.2210/pdb2n24/pdb
• NMR Information: BMRB: 25585
• Descriptor: O2_contryphan_Vc1 (1 entity in total)
• Functional Keywords: contryphan-vc1, single disulfide-directed beta hairpin, sdh, toxin
• Biological source: Conus victoriae (Queen Victoria cone)
• Total number of polymer chains: 1
• Total formula weight: 3557.96

Authors

Robinson, S.D.,Chhabra, S.,Norton, R.S. (deposition date: 2015-04-27, release date: 2016-02-03, Last modification date: 2024-10-30)

Primary citation

Robinson, S.D.,Chhabra, S.,Belgi, A.,Chittoor, B.,Safavi-Hemami, H.,Robinson, A.J.,Papenfuss, A.T.,Purcell, A.W.,Norton, R.S.
A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed beta-Hairpin Fold.
Structure, 24:293-299, 2016

PubMed Abstract: Certain peptide folds, owing to a combination of intrinsic stability and resilience to amino acid substitutions, are particularly effective for the display of diverse functional groups. Such "privileged scaffolds" are valuable as starting points for the engineering of new bioactive molecules. We have identified a precursor peptide expressed in the venom gland of the marine snail Conus victoriae, which appears to belong to a hitherto undescribed class of molluscan neuropeptides. Mass spectrometry matching with the venom confirmed the complete mature peptide sequence as a 31-residue peptide with a single disulfide bond. Solution structure determination revealed a unique peptide fold that we have designated the single disulfide-directed β hairpin (SDH). The SDH fold is highly resistant to thermal denaturation and forms the core of several other multiple disulfide-containing peptide folds, including the inhibitor cystine knot. This elementary fold may offer a valuable starting point for the design and engineering of new bioactive peptides.

PubMed: 26774129
DOI: 10.1016/j.str.2015.11.015

Experimental method

SOLUTION NMR