{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hollas H"],"funding":["Norges Forskningsråd","Helse Vest","Universität Heidelberg"],"pagination":["4492-4504"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9748365"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(23)"],"pubmed_abstract":["Annexins (Anxs) are a family of highly homologous proteins that bind and aggregate lipid vesicles in the presence of calcium. All members of the family contain a variable N-terminus determining specific functions, followed by a conserved core region responsible for the general calcium-dependent lipid-binding property. The core structure consists of four homologous domains (D<sub>I</sub>-D<sub>IV</sub>), each consisting of a right-handed super-helix of five α-helices. We present data from a combination of site-directed mutagenesis, NMR, and circular dichroism showing that the G25-D34 region of the N-terminus as well as the contacts between residues D38A, R63A, and Q67A of AnxA2-D<sub>I</sub> are crucial for the autonomous folding and stability of D<sub>I</sub> of AnxA2. However, we also sho"],"journal":["Biophysical journal"],"pubmed_title":["The cooperative folding of annexin A2 relies on a transient nonnative intermediate."],"pmcid":["PMC9748365"],"funding_grant_id":["199747","911499"],"pubmed_authors":["Ramirez J","Hollas H","Gianni S","Vedeler A","Nomine Y","Trave G","Kostmann C","Toto A"],"additional_accession":[]},"is_claimable":false,"name":"The cooperative folding of annexin A2 relies on a transient nonnative intermediate.","description":"Annexins (Anxs) are a family of highly homologous proteins that bind and aggregate lipid vesicles in the presence of calcium. All members of the family contain a variable N-terminus determining specific functions, followed by a conserved core region responsible for the general calcium-dependent lipid-binding property. The core structure consists of four homologous domains (D<sub>I</sub>-D<sub>IV</sub>), each consisting of a right-handed super-helix of five α-helices. We present data from a combination of site-directed mutagenesis, NMR, and circular dichroism showing that the G25-D34 region of the N-terminus as well as the contacts between residues D38A, R63A, and Q67A of AnxA2-D<sub>I</sub> are crucial for the autonomous folding and stability of D<sub>I</sub> of AnxA2. However, we also sho","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-28T01:34:46.135Z","creation":"2025-04-05T22:22:30.406Z"},"accession":"S-EPMC9748365","cross_references":{"pubmed":["36325614"],"doi":["10.1016/j.bpj.2022.10.043"]}}