On the structure and function of apolipoproteins: more than a family of lipid-binding proteins.
Exchangeable apolipoproteins have been the subject of intense biomedical investigation for decades. However, only in recent years the elucidation of the three-dimensional structure reported for several members of the apolipoprotein family has provided insights into their functions at a molecular level for the first time. Moreover, the role of exchangeable apolipoproteins in several cellular events distinct from lipid metabolism has recently been described. This review summarizes these contributions, which have not only allowed the identification of the apolipoprotein domains that determine substrate binding specificity and/or affinity but also the plausible molecular mechanism(s) involved.
Bolanos-Garcia
Victor Martin
VM
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. victor@cryst.bioc.cam.ac.uk
Miguel
Ricardo Nunez
RN
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001053:Apolipoproteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D007700:Kinetics; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D008074:Lipoproteins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D020365:RNA Helicases; D013329:Structure-Activity Relationship; D015534:Trans-Activators
D000682:Amyloid; D001053:Apolipoproteins; D008055:Lipids; D008074:Lipoproteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D015534:Trans-Activators; D020365:RNA Helicases; C101828:UPF1 protein, human