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PXD024519 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleXL-MS analysis of human tyrosine hydroxylase
DescriptionTyrosine hydroxylase (TH) is a highly regulated enzyme that catalyses the rate-limiting step in the biosynthesis of dopamine (DA) and other catecholamines. Mutations and dysfunction in this enzyme lead to DA deficiency and parkinsonisms of different severity. An understanding of TH deficiency at the level of structure and stability has been lacking to date, as only structures of truncated TH forms have been available. Here, we used cryoEM and XL-MS to determine the high-resolution structure of full-length human tetrameric TH in the absence and presence of the end-product and feedback inhibitor DA bound to the active site
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMiguel Marcilla
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentTripleTOF 5600
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-03-04 03:58:14ID requested
12021-12-22 02:31:17announced
Publication List
Lorente E, Marcilla M, de la Sota PG, Quijada-Freire A, Mir C, L, รณ, pez D, Acid Stripping after Infection Improves the Detection of Viral HLA Class I Natural Ligands Identified by Mass Spectrometry. Int J Mol Sci, 22(19):(2021) [pubmed]
Keyword List
submitter keyword: XL-MS, BS3, Tyrosine hydroxylase, Dopamine
Contact List
Fernando Corrales
contact affiliationProteomics Unit. Spanish National Biotechnology Centre. CNB-CSIC
contact emailfcorrales@cnb.csic.es
lab head
Miguel Marcilla
contact affiliationProteomics Unit - Dpt. of Macromolecular Structures - Spanish National Biotechnolgy Centre (CNB-CSIC)
contact emailmmarcilla@cnb.csic.es
dataset submitter
Full Dataset Link List
Dataset FTP location
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