{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dolinska MB"],"funding":["Intramural NIH HHS","National Institutes of Health"],"pagination":["e4518"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9793978"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(1)"],"pubmed_abstract":["Tyrosinase related protein 1 (TYRP1) is the most abundant melanosomal protein of the melanocyte, where plays an important role in the synthesis of eumelanin, possibly catalyzing the oxidation of 5,6-dihydroxyindole-2-carboxylic acid to 5,6-quinone-2-carboxylic acid. Mutations to the TYRP1 gene can result in oculocutaneous albinism type 3 (OCA3), a rare disease characterized by reduced synthesis of melanin in skin, hair, and eyes. To investigate the effect of genetic mutations on the TYRP1 structure, function, and stability, we engineered the intramelanosomal domain of TYRP1 and its mutant variants mimicking either OCA3-related changes, C30R, H215Y, D308N, and R326H or R87G mutant variant, analogous to OCA1-related pathogenic effect in tyrosinase. Proteins were produced in Trichoplusia Ni l"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["In vitro characterization of the intramelanosomal domain of human recombinant TYRP1 and its oculocutaneous albinism type 3-related mutant variants."],"pmcid":["PMC9793978"],"funding_grant_id":["ZIA EY000476‐10","ZIA EY000476"],"pubmed_authors":["Anderson DE","Sergeev YV","Dolinska MB"],"additional_accession":[]},"is_claimable":false,"name":"In vitro characterization of the intramelanosomal domain of human recombinant TYRP1 and its oculocutaneous albinism type 3-related mutant variants.","description":"Tyrosinase related protein 1 (TYRP1) is the most abundant melanosomal protein of the melanocyte, where plays an important role in the synthesis of eumelanin, possibly catalyzing the oxidation of 5,6-dihydroxyindole-2-carboxylic acid to 5,6-quinone-2-carboxylic acid. Mutations to the TYRP1 gene can result in oculocutaneous albinism type 3 (OCA3), a rare disease characterized by reduced synthesis of melanin in skin, hair, and eyes. To investigate the effect of genetic mutations on the TYRP1 structure, function, and stability, we engineered the intramelanosomal domain of TYRP1 and its mutant variants mimicking either OCA3-related changes, C30R, H215Y, D308N, and R326H or R87G mutant variant, analogous to OCA1-related pathogenic effect in tyrosinase. Proteins were produced in Trichoplusia Ni l","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-28T01:55:15.357Z","creation":"2025-04-04T19:00:37.267Z"},"accession":"S-EPMC9793978","cross_references":{"pubmed":["36412553"],"doi":["10.1002/pro.4518"]}}