8V2M

Structure of Asterias rubens peptide (KASH2)

8V2M の概要

• エントリーDOI: 10.2210/pdb8v2m/pdb
• NMR情報: BMRB: 31128
• 分子名称: Kartesh 2 (1 entity in total)
• 機能のキーワード: protein, unknown function
• 由来する生物種: Asterias rubens (European starfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3082.49

構造登録者

Takjoo, R.,Daly, N.L. (登録日: 2023-11-23, 公開日: 2024-11-27, 最終更新日: 2025-03-19)

主引用文献

Takjoo, R.,Wilson, D.T.,Le Quilliec, J.,Schmidt, C.A.,Zhao, G.,Liddell, M.J.,Shaikh, N.Y.,Sunagar, K.,Loukas, A.,Smout, M.J.,Daly, N.L.
Structural analysis of an Asterias rubens peptide indicates the presence of a disulfide-directed beta-hairpin fold.
Febs Open Bio, 15:415-426, 2025

PubMed Abstract: Sea stars are an abundant group of marine invertebrates that display remarkably robust regenerative capabilities throughout all life stages. Numerous proteins and peptides have been identified in a proteome study on the coelomic fluid (biofluid) of the common sea star Asterias rubens, which appear to be involved with the wound-healing response in the organism. However, the three-dimensional structure and function of several of these injury-responsive peptides, including the peptide KASH2, are yet to be investigated. Here, we show that the KASH2 peptide adopts a disulfide-directed β-hairpin fold (DDH). The DDH motif appears to be evolutionarily related to the inhibitor cystine knot motif, which is one of the most widespread disulfide-rich peptide folds. The DDH motif was originally thought to be restricted to arachnids, but our study suggests that as a result of convergent evolution it could also have originated in sea stars. Although the widely conserved DDH fold has potential cross-phyla wound-healing capacity, we have shown that KASH2 does not enhance the proliferation of human fibroblasts, a simple method for wound-healing re-epithelialisation screening. Therefore, additional research is necessary to determine the role of KASH2 in the sea stars.

PubMed: 39561265
DOI: 10.1002/2211-5463.13931

実験手法

SOLUTION NMR