Proteomics

Dataset Information

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Apolipoprotein A1 forms 5/5 and 5/4 antiparallel dimers in human high-density lipoprotein


ABSTRACT: We performed zero-order chemical cross-linking mass spectrometry experiments on reconstituted discoidal HDL and human HDL to determine the APOA1 orientations in these particles.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Yi He  

LAB HEAD: Jay W Heinecke

PROVIDER: PXD009927 | Pride | 2019-04-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
APOA1dimers.xlsx Xlsx
HDL_EDC_01.raw Raw
HDL_EDC_02.raw Raw
HDL_EDC_03.raw Raw
HDL_EDC_04.raw Raw
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Publications

Apolipoprotein A1 Forms 5/5 and 5/4 Antiparallel Dimers in Human High-density Lipoprotein.

He Yi Y   Song Hyun D HD   Anantharamaiah G M GM   Palgunachari M N MN   Bornfeldt Karin E KE   Segrest Jere P JP   Heinecke Jay W JW  

Molecular & cellular proteomics : MCP 20190118 5


Apolipoprotein A1 (APOA1), the major protein of high-density lipoprotein (HDL), contains 10 helical repeats that play key roles in protein-protein and protein-lipid interactions. The current structural model for HDL proposes that APOA1 forms an antiparallel dimer in which helix 5 in monomer 1 associates with helix 5 in monomer 2 along a left-left (LL5/5) interface, forming a protein complex with a 2-fold axis of symmetry centered on helix 5. However, computational studies suggest that other orie  ...[more]

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