Proteomics

Dataset Information

0

Confirmation of the binding site of spermine to ATP13A2 protein


ABSTRACT: To better understand human ATP13A2-mediated polyamine transport, we used single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2. Interestingly, we found polyamine binding at multiple sites distributed along the transmembrane regions in ATP13A2 protein, which has not been reported in previous studies. Therefore, we used cross-linking mass spectrometry (CX-MS) to confirm potential binding sites.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: jianqiang Mu  

LAB HEAD: Zhongmin LIU

PROVIDER: PXD037493 | Pride | 2023-05-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ATP13A2-WT_Crosslink.csv Csv
ATP13A2-WT_Looplink.csv Csv
ATP13A2-WT_Monolink.csv Csv
ATP13A2-WT_SPM.csv Csv
ATP13A2_Q9NQ11-1_.fasta Fasta
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Publications


Dysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a transporter with a critical role in balancing the polyamine concentration between the lysosome and the cytosol. Here, to better understand human ATP13A2-mediated polyamine transport, we use single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2 in six intermediate  ...[more]

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