The Journal of Membrane Biology

, Volume 252, Issue 1, pp 41–60 | Cite as

Significance of Cholesterol-Binding Motifs in ABCA1, ABCG1, and SR-B1 Structure

  • Alexander D. DergunovEmail author
  • Eugeny V. Savushkin
  • Liudmila V. Dergunova
  • Dmitry Y. Litvinov


ABCA1, ABCG1 transporters, and SR-B1 receptor are the major proteins involved in cholesterol efflux from cells. We superposed in silico the location of putative cholesterol (Chol)-binding motifs CRAC/CARC and CCM in human ABCA1, ABCG1, and SR-B1 with (1) transmembrane protein topology, (2) a profile of structural order of protein, and (3) with an influence of single amino acid substitutions on protein structure and function. ABCA1, ABCG1, and SR-B1 molecules contain 50, 19, and 13 Chol-binding motifs, respectively, that are localized either in membrane helices, or at membrane–water interface, or in water-exposed protein regions. Arginine residues in motifs that coincide with molecular recognition features within intrinsically disordered regions of the transporters are suggested to be important in cholesterol binding; cholesterol–arginine interaction may result in the induction of local order in protein structure. Chol-binding motifs in membrane helices may immobilize cholesterol, while motifs at membrane–water interface may be involved into the efflux of “active” cholesterol. Cholesterol may interfere with ATP binding in both nucleotide-binding domains of ABCA1 structure. For ABCA1 and ABCG1, but not for SR-B1, the presence of mirror code as a CARC–CRAC vector couple in the C-terminal helices controlling protein–cholesterol interactions in the outer and inner membrane leaflets was evidenced. We propose the role of Chol-binding motifs with different immersion in membrane in transport of different cholesterol pools by ABCA1 and ABCG1.


ABCA1 ABCG1 SR-B1 ApoA-I Cholesterol-binding domains 



Apolipoprotein A-I


Inverted CRAC


Cholesterol consensus motif




Cholesterol recognition/interaction amino acid consensus


High-density lipoproteins


HDL cholesterol


Human gene mutation database


Molecular recognition feature


Nucleotide-binding domain


Single-nucleotide polymorphism




Transmembrane domain



This study was funded by the grants 16-04-00067 and 17-04-00217 from the Russian Fund for Basic Research.

Compliance with Ethical Standards

Conflict of interest

The authors declare that they have no conflict of interest.

Research Involving Human and Animal Participants

This article does not contain any studies with human participants or animals performed by any of the authors.


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Authors and Affiliations

  1. 1.National Research Centre for Preventive MedicineMoscowRussia
  2. 2.Institute of Molecular Genetics of the Russian Academy of Sciences2 Kurchatov Square, MoscowRussia

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