Solution structure of bovine heart fatty acid-binding protein (H-FABPC)

Lassen, Dirck; Lücke, Christian; Kromminga, Arno; Lezius, Axel G.; Spener, Friedrich; Rüterjans, Heinz

doi:10.1007/978-1-4615-3096-1_3

Cited by 4 publications

(6 citation statements)

References 17 publications

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“…Furthermore, they are similar to results of energy minimizations of cellular retinol-binding protein, in which helix II and the βC-βD and βE-βF loops were most variant (26). Modeled, energyminimized, and crystallographic data demonstrating mobility in these specific protein regions are supported by NMR solution structural data for apo and holo heart FABP (27)(28)(29), as well as apo and holo rat intestinal FABP (30)(31)(32), human intestinal FABP (33), and the ileal lipid-binding protein (34), all of which vary most in composite structures at helix II, and the βC-βD and βE-βF loops. Helix II in the apo IFABP NMR solution structure is largely disordered in random coil, only developing helical character upon binding of a ligand, at which time it adopts the familiar R-helical structure observed in holo crystals.…”

Section: Discussionsupporting

confidence: 72%

Analysis of a Series of Phenylalanine 57 Mutants of the Adipocyte Lipid-Binding Protein

Simpson

Bernlohr

1998

Biochemistry

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The importance of phenylalanine 57, an adipocyte lipid-binding protein (ALBP) portal residue, to ligand affinity and specificity has been investigated using a series of ALBP position 57 mutants. In wild-type ALBP, phenylalanine 57 undergoes a side chain rotation upon ligand binding, moving from an inwardly oriented, ligand-exclusive position in apoprotein structures to an outwardly oriented position in the holoprotein. To examine the role of F57 side chain rotation in the apoprotein-holoprotein transition and in ligand selectivity, ALBP site-specific mutants F57A, F57G, F57H, and F57W were expressed in Escherichia coli and purified to homogeneity. Mutants were analyzed for binding characteristics and stability toward chemical denaturation, and energy-minimized models of each mutant were constructed using apo, oleate-, and arachidonate-bound ALBP crystallographic coordinates. The stability of ALBP forms (wtALBP approximately F57G > F57A > F57W > F57H) was unrelated to the affinity of ALBP forms (wtALBP approximately F57W > F57H > F57G > F57A) for various lipids and did not vary between fatty acids. Since ligand selectivity was maintained between wild type and all mutants while ligand affinity was grossly diminished, we conclude that phenylalanine 57 is critical to the formation of the fatty acid/ALBP complex, but is uninvolved in determination of selectivity over the range of physiological ligands tested.

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Section: Discussionsupporting

confidence: 72%

Analysis of a Series of Phenylalanine 57 Mutants of the Adipocyte Lipid-Binding Protein

Simpson

Bernlohr

1998

Biochemistry

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“…For the pI 4.9 isoform, multiple peaks were observed at positions 22 to 36, 53 to 60 and 119 to 122 (Lü cke et al, 1992). Based on these findings, it was concluded that helix II and adjacent portions of the molecule maintain four distinct backbone conformations with lifetimes of at least 10 ms (Lassen et al, 1993). Multiple peaks were also observed for the pI 5.1 isoform at positions 2, 3, 6, 30 to 34, 36, 53 to 60, 75 to 76, 88 to 90, 100, 101 and 122 (Lassen et al, 1995).…”

Section: Comparison To the Structures Of Homologous Proteinsmentioning

confidence: 92%

“…This protein shares 30% sequence identity with rat I-FABP. The H-FABP structure was based initially on 1071 restraints derived from 2-D 1 H spectra of an unenriched sample (Lü cke et al, 1992;Lassen et al, 1993) and subsequently, 2371 restraints derived from 2-D 1 H and 3-D 15 N-resolved spectra of a uniformly 15 N-enriched sample (Lassen et al, 1995). The overall fold was the same as observed here for I-FABP, but some differences were noted in the conformation of the bound ligand and several other regions of the protein.…”

Section: Comparison To the Structures Of Homologous Proteinsmentioning

confidence: 93%

The NMR Solution Structure of Intestinal Fatty Acid-binding Protein Complexed with Palmitate: Application of a Novel Distance Geometry Algorithm

Hodsdon

Ponder

Cistola

1996

Journal of Molecular Biology

163

155

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“…Branched-chain fatty acids, isoprenoids derived from cleavage of chlorophyll side chain (rev. in [20,61], are nuclear signaling molecules representing the most potent endogenous inducers of peroxisome proliferator activated receptors known [62][63][64][65][66][67]. Finally, SCP-2 also facilitates the peroxisomal oxidation of the branched-side chain of cholesterol to form bile acids [1,20,68].…”

Section: Lipids Involved In Intracellular Signalingmentioning

confidence: 99%

Sterol carrier protein-2: New roles in regulating lipid rafts and signaling

Schroeder

Atshaves

McIntosh

et al. 2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Sterol carrier protein-2 (SCP-2) was independently discovered as a soluble protein that binds and transfers cholesterol as well as phospholipids (nonspecific lipid transfer protein, nsLTP) in vitro. Physiological functions of this protein are only now beginning to be resolved. The gene encoding SCP-2 also encodes sterol carrier protein-x (SCP-x) arising from an alternate transcription site. In vitro and in vivo SCP-x serves as a peroxisomal 3-ketoacyl-CoA thiolase in oxidation of branchedchain lipids (cholesterol to form bile acids; branched-chain fatty acid for detoxification). While peroxisomal SCP-2 facilitates branched-chain lipid oxidation, the role(s) of extraperoxisomal (up to 50% of total) are less clear. Studies using transfected fibroblasts overexpressing SCP-2 and hepatocytes from SCP-2/SCP-x gene-ablated mice reveal that SCP-2 selectively remodels the lipid composition, structure, and function of lipid rafts/caveolae. Studies of purified SCP-2 and in cells show that SCP-2 has high affinity for and selectively transfers many lipid species involved in intracellular signaling: fatty acids, fatty acyl CoAs, lysophosphatidic acid, phosphatidylinositols, and sphingolipids (sphingomyelin, ceramide, mono-di-and multi-hexosylceramides, gangliosides). SCP-2 selectively redistributes these signaling lipids between lipid rafts/caveolae and intracellular sites. These findings suggest SCP-2 serves not only in cholesterol and phospholipid transfer, but also in regulating multiple lipid signaling pathways in lipid raft/caveolae microdomains of the plasma membrane.

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Solution structure of bovine heart fatty acid-binding protein (H-FABPC)

Cited by 4 publications

References 17 publications

Analysis of a Series of Phenylalanine 57 Mutants of the Adipocyte Lipid-Binding Protein

Analysis of a Series of Phenylalanine 57 Mutants of the Adipocyte Lipid-Binding Protein

The NMR Solution Structure of Intestinal Fatty Acid-binding Protein Complexed with Palmitate: Application of a Novel Distance Geometry Algorithm

Sterol carrier protein-2: New roles in regulating lipid rafts and signaling

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