8V2U
Structure of Asterias rubens peptide KASH2-amide
Summary for 8V2U
| Entry DOI | 10.2210/pdb8v2u/pdb |
| Related | 8V2M |
| NMR Information | BMRB: 31129 |
| Descriptor | Kartesh 2 (1 entity in total) |
| Functional Keywords | asterias rubens peptide, unknown function |
| Biological source | Asterias rubens (European starfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 2894.26 |
| Authors | Takjoo, R.,Le Quilliec, J.,Daly, N.L. (deposition date: 2023-11-23, release date: 2024-11-27, Last modification date: 2025-03-19) |
| Primary citation | 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 Cited by 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: 39561265DOI: 10.1002/2211-5463.13931 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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