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@ARTICLE{Wu:18200,
author = {Wu, Z. and Gogonea, V. and Lee, X. and May, R.P. and
Pipich, V. and Wagner, M.A. and Undurti, A. and Tallant,
T.C. and Baleanu-Gogonea, C. and Charlton, F. and Ioffe, A.
and DiDonato, J.A. and Rye, K--A. and Hazen, S.L.},
title = {{T}he low resolution structure of {A}po{A}1 in spherical
high density lipoprotein revealed by small angle neutron
scattering},
journal = {The journal of biological chemistry},
volume = {286},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {PreJuSER-18200},
year = {2011},
note = {This work was supported, in whole or in part, by National
Institutes of Health Grants P01 HL098055, P01
HL076491-055328, and P01 HL087018-02001. This work was also
supported in part by a grant from the Foundation Leducq.},
abstract = {Spherical high density lipoprotein (sHDL), a key player in
reverse cholesterol transport and the most abundant form of
HDL, is associated with cardiovascular diseases. Small angle
neutron scattering with contrast variation was used to
determine the solution structure of protein and lipid
components of reconstituted sHDL. Apolipoprotein A1, the
major protein of sHDL, forms a hollow structure that cradles
a central compact lipid core. Three apoA1 chains are
arranged within the low resolution structure of the protein
component as one of three possible global architectures: (i)
a helical dimer with a hairpin (HdHp), (ii) three hairpins
(3Hp), or (iii) an integrated trimer (iT) in which the three
apoA1 monomers mutually associate over a portion of the sHDL
surface. Cross-linking and mass spectrometry analyses help
to discriminate among the three molecular models and are
most consistent with the HdHp overall architecture of apoA1
within sHDL.},
keywords = {Apolipoprotein A-I: chemistry / Humans / Lipoproteins, HDL:
chemistry / Mass Spectrometry / Neutrons / Protein
Multimerization / Scattering, Small Angle / Apolipoprotein
A-I (NLM Chemicals) / Lipoproteins, HDL (NLM Chemicals) / J
(WoSType)},
cin = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
Science JCNS (München) ; JCNS-FRM-II / JCNS-1 / JCNS-2 /
Jülich Centre for Neutron Science JCNS (JCNS) ; JCNS /
PGI-4},
ddc = {570},
cid = {I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106 /
I:(DE-Juel1)JCNS-20121112 / I:(DE-Juel1)PGI-4-20110106},
pnm = {BioSoft: Makromolekulare Systeme und biologische
Informationsverarbeitung / Großgeräte für die Forschung
mit Photonen, Neutronen und Ionen (PNI)},
pid = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
experiment = {EXP:(DE-MLZ)KWS2-20140101},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21292766},
pmc = {pmc:PMC3069452},
UT = {WOS:000289077500063},
doi = {10.1074/jbc.M110.209130},
url = {https://juser.fz-juelich.de/record/18200},
}