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A saposin-lipoprotein nanoparticle system for membrane proteins

Frauenfeld, Jens (author)
Loving, Robin (author)
Armache, Jean-Paul (author)
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Sonnen, Andreas F-P (author)
Guettou, Fatma (author)
Moberg, Per (author)
Zhu, Lin (author)
KTH,Hälso- och systemvetenskap
Jegerschöld, Caroline (author)
KTH,Strukturell bioteknik
Flayhan, Ali (author)
Briggs, John A. G. (author)
Garoff, Henrik (author)
Low, Christian (author)
Cheng, Yifan (author)
Nordlund, Par (author)
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 (creator_code:org_t)
Nature Publishing Group, 2016
2016
English.
In: Nature Methods. - : Nature Publishing Group. - 1548-7091 .- 1548-7105. ; 13:4, s. 345-351
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • A limiting factor in membrane protein research is the ability to solubilize and stabilize such proteins. Detergents are used most often for solubilizing membrane proteins, but they are associated with protein instability and poor compatibility with structural and biophysical studies. Here we present a saposin-lipoprotein nanoparticle system, Salipro, which allows for the reconstitution of membrane proteins in a lipid environment that is stabilized by a scaffold of saposin proteins. We demonstrate the applicability of the method on two purified membrane protein complexes as well as by the direct solubilization and nanoparticle incorporation of a viral membrane protein complex from the virus membrane. Our approach facilitated high-resolution structural studies of the bacterial peptide transporter PeptT(S02) by single-particle cryo-electron microscopy (cryo-EM) and allowed us to stabilize the HIV envelope glycoprotein in a functional state.

Subject headings

NATURVETENSKAP  -- Biologi -- Biofysik (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biophysics (hsv//eng)

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ref (subject category)
art (subject category)

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