This title appears in the Scientific Report : 2011 

The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering
Wu, Z.
Gogonea, V. / Lee, X. / May, R.P. / Pipich, V. / Wagner, M.A. / Undurti, A. / Tallant, T.C. / Baleanu-Gogonea, C. / Charlton, F. / Ioffe, A. / DiDonato, J.A. / Rye, K--A. / Hazen, S.L.
Streumethoden; JCNS-2
Neutronenstreuung; JCNS-1
JCNS-FRM-II; JCNS-FRM-II
Neutronenstreuung; ICS-1
Streumethoden; PGI-4
JCNS; JCNS
The @journal of biological chemistry, 286 (2011)
Bethesda, Md. Soc. 2011
21292766
10.1074/jbc.M110.209130
Journal Article
Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
Journal of Biological Chemistry 286
J
Please use the identifier: http://dx.doi.org/10.1074/jbc.M110.209130 in citations.
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.