{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Takjoo R"],"funding":["Merchant Foundation","National Cancer Institute","NCI NIH HHS","National Institutes of Health","DBT/Wellcome Trust India Alliance","Wellcome Trust","NIH HHS","Australian Research Council","James Cook University"],"pagination":["415-426"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11891777"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(3)"],"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 "],"journal":["FEBS open bio"],"pubmed_title":["Structural analysis of an Asterias rubens peptide indicates the presence of a disulfide-directed β-hairpin fold."],"pmcid":["PMC11891777"],"funding_grant_id":["FF110100226","R01CA164719","LE160100218","IA/I/19/2/504647","R01 CA164719"],"pubmed_authors":["Takjoo R","Schmidt CA","Smout MJ","Wilson DT","Daly NL","Liddell MJ","Shaikh NY","Le Quilliec J","Zhao G","Sunagar K","Loukas A"],"additional_accession":[]},"is_claimable":false,"name":"Structural analysis of an Asterias rubens peptide indicates the presence of a disulfide-directed β-hairpin fold.","description":"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 ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-01T20:12:20.564Z","creation":"2025-04-07T07:49:15.483Z"},"accession":"S-EPMC11891777","cross_references":{"pubmed":["39561265"],"doi":["10.1002/2211-5463.13931"]}}