2N24

Solution NMR structure of Contryphan-Vc1

2N24 の概要

• エントリーDOI: 10.2210/pdb2n24/pdb
• NMR情報: BMRB: 25585
• 分子名称: O2_contryphan_Vc1 (1 entity in total)
• 機能のキーワード: contryphan-vc1, single disulfide-directed beta hairpin, sdh, toxin
• 由来する生物種: Conus victoriae (Queen Victoria cone)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3557.96

構造登録者

Robinson, S.D.,Chhabra, S.,Norton, R.S. (登録日: 2015-04-27, 公開日: 2016-02-03, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR