{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nayak AR"],"funding":["National Institutes of Health National Cancer Institute","New Jersey Health Foundation","NCI NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["108466"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12059335"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["301(5)"],"pubmed_abstract":["Maackia amurensis lectins, including MASL, MAA, and MAL2, are widely utilized in biochemical and medicinal research. However, the structural and functional differences between these lectins have not been defined. Here, we present a high-resolution cryo-EM structure of MASL revealing that its tetrameric assembly is directed by two intersubunit disulfide bridges. These bridges, formed by C272 residues, are central to the dimer-of-dimers assembly of a MASL tetramer. This cryo-EM structure also identifies residues involved in stabilizing the dimer interface, multiple glycosylation sites, and calcium and manganese atoms in the sugar-binding pockets of MASL. Notably, our analysis reveals that Y250 in the carbohydrate-binding site of MASL adopts a flipped conformation, likely acting as a gatekeep"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Maackia amurensis seed lectin structure and sequence comparison with other M. amurensis lectins."],"pmcid":["PMC12059335"],"funding_grant_id":["1R41CA268160-01A1","1R15CA271044-01","P30 CA056036","R41 CA268160","S10 OD030457","2P30CA056036","PC78-24NIH","R15 CA271044"],"pubmed_authors":["Zheng H","Zhao C","Temiakov D","Nicoletto RE","Nayak AR","Holdcraft CJ","Yin AC","Goldberg GS"],"additional_accession":[]},"is_claimable":false,"name":"Maackia amurensis seed lectin structure and sequence comparison with other M. amurensis lectins.","description":"Maackia amurensis lectins, including MASL, MAA, and MAL2, are widely utilized in biochemical and medicinal research. However, the structural and functional differences between these lectins have not been defined. Here, we present a high-resolution cryo-EM structure of MASL revealing that its tetrameric assembly is directed by two intersubunit disulfide bridges. These bridges, formed by C272 residues, are central to the dimer-of-dimers assembly of a MASL tetramer. This cryo-EM structure also identifies residues involved in stabilizing the dimer interface, multiple glycosylation sites, and calcium and manganese atoms in the sugar-binding pockets of MASL. Notably, our analysis reveals that Y250 in the carbohydrate-binding site of MASL adopts a flipped conformation, likely acting as a gatekeep","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-02T06:48:43.008Z","creation":"2026-04-15T03:15:30.596Z"},"accession":"S-EPMC12059335","cross_references":{"pubmed":["40158854"],"doi":["10.1016/j.jbc.2025.108466"]}}