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PDBsum entry 1alb
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Lipid binding protein
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PDB id
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1alb
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
31:3484-3492
(1992)
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PubMed id:
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Crystal structure of recombinant murine adipocyte lipid-binding protein.
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Z.Xu,
D.A.Bernlohr,
L.J.Banaszak.
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ABSTRACT
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Adipocyte lipid-binding protein (ALBP) is the adipocyte member of an
intracellular hydrophobic ligand-binding protein family. ALBP is phosphorylated
by the insulin receptor kinase upon insulin stimulation. The crystal structure
of recombinant murine ALBP has been determined and refined to 2.5 A. The final R
factor for the model is 0.18 with good canonical properties. Crystalline ALBP
has a conformation which is essentially identical to that of intestinal fatty
acid binding protein and myelin P2 protein. Although the crystal structure is of
the apo- form, a cavity resembling that in other family members is present. It
contains a number of bound and implied unbound water molecules and shows no
large obvious portal to the external milieu. The cavity of ALBP, which by
homology is the ligand-binding site, is formed by both polar and hydrophobic
residues among which is tyrosine 19. Y19 is phosphorylated by the insulin
receptor kinase as described in the accompanying paper [Buelt, M. K., Xu, Z.,
Banaszak, L. J., & Bernlohr, D. A. (1992) Biochemistry (following paper in
this issue)]. By comparing ALBP with the earlier structural results on
intestinal fatty acid binding protein, it is now possible to delineate conserved
amino acids which help form the binding site in this family.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.V.Hertzel,
K.Hellberg,
J.M.Reynolds,
A.C.Kruse,
B.E.Juhlmann,
A.J.Smith,
M.A.Sanders,
D.H.Ohlendorf,
J.Suttles,
and
D.A.Bernlohr
(2009).
Identification and characterization of a small molecule inhibitor of Fatty Acid binding proteins.
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J Med Chem,
52,
6024-6031.
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PDB code:
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T.Koeck,
B.Willard,
J.W.Crabb,
M.Kinter,
D.J.Stuehr,
and
K.S.Aulak
(2009).
Glucose-mediated tyrosine nitration in adipocytes: targets and consequences.
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Free Radic Biol Med,
46,
884-892.
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F.Torta,
L.Elviri,
M.Careri,
A.Mangia,
D.Cavazzini,
and
G.L.Rossi
(2008).
Mass spectrometry and hydrogen/deuterium exchange measurements of alcohol-induced structural changes in cellular retinol-binding protein type I.
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Rapid Commun Mass Spectrom,
22,
330-336.
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E.Erbay,
H.Cao,
and
G.S.Hotamisligil
(2007).
Adipocyte/macrophage fatty acid binding proteins in metabolic syndrome.
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Curr Atheroscler Rep,
9,
222-229.
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M.Mihajlovic,
and
T.Lazaridis
(2007).
Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane.
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Protein Sci,
16,
2042-2055.
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S.M.Maté,
J.P.Layerenza,
and
A.Ves-Losada
(2007).
Incorporation of arachidonic and stearic acids bound to L-FABP into nuclear and endonuclear lipids from rat liver cells.
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Lipids,
42,
589-602.
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D.L.Lynch,
and
P.H.Reggio
(2006).
Cannabinoid CB1 receptor recognition of endocannabinoids via the lipid bilayer: molecular dynamics simulations of CB1 transmembrane helix 6 and anandamide in a phospholipid bilayer.
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J Comput Aided Mol Des,
20,
495-509.
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R.F.Fischetti,
D.J.Rodi,
D.B.Gore,
and
L.Makowski
(2004).
Wide-angle X-ray solution scattering as a probe of ligand-induced conformational changes in proteins.
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Chem Biol,
11,
1431-1443.
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M.Kurz,
V.Brachvogel,
H.Matter,
S.Stengelin,
H.Thüring,
and
W.Kramer
(2003).
Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures.
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Proteins,
50,
312-328.
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PDB codes:
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C.Lücke,
F.Zhang,
J.A.Hamilton,
J.C.Sacchettini,
and
H.Rüterjans
(2000).
Solution structure of ileal lipid binding protein in complex with glycocholate.
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Eur J Biochem,
267,
2929-2938.
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PDB code:
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R.Najmanovich,
J.Kuttner,
V.Sobolev,
and
M.Edelman
(2000).
Side-chain flexibility in proteins upon ligand binding.
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Proteins,
39,
261-268.
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E.Schievano,
S.Mammi,
and
E.Peggion
(1999).
Determination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.
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Biopolymers,
50,
1.
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T.B.Woolf
(1998).
Simulations of fatty acid-binding proteins suggest sites important for function. I. Stearic acid.
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Biophys J,
74,
681-693.
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V.J.LiCata,
and
D.A.Bernlohr
(1998).
Surface properties of adipocyte lipid-binding protein: Response to lipid binding, and comparison with homologous proteins.
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Proteins,
33,
577-589.
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D.A.Bernlohr,
M.A.Simpson,
A.V.Hertzel,
and
L.J.Banaszak
(1997).
Intracellular lipid-binding proteins and their genes.
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Annu Rev Nutr,
17,
277-303.
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J.Ory,
C.D.Kane,
M.A.Simpson,
L.J.Banaszak,
and
D.A.Bernlohr
(1997).
Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein.
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J Biol Chem,
272,
9793-9801.
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PDB codes:
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C.Lücke,
F.Zhang,
H.Rüterjans,
J.A.Hamilton,
and
J.C.Sacchettini
(1996).
Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein.
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Structure,
4,
785-800.
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PDB code:
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M.R.Rich,
and
J.S.Evans
(1996).
Molecular dynamics simulations of adipocyte lipid-binding protein: effect of electrostatics and acyl chain unsaturation.
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Biochemistry,
35,
1506-1515.
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M.Tendler,
C.A.Brito,
M.M.Vilar,
N.Serra-Freire,
C.M.Diogo,
M.S.Almeida,
A.C.Delbem,
J.F.Da Silva,
W.Savino,
R.C.Garratt,
N.Katz,
and
A.S.Simpson
(1996).
A Schistosoma mansoni fatty acid-binding protein, Sm14, is the potential basis of a dual-purpose anti-helminth vaccine.
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Proc Natl Acad Sci U S A,
93,
269-273.
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D.H.Shin,
J.Y.Lee,
K.Y.Hwang,
K.K.Kim,
and
S.W.Suh
(1995).
High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings.
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Structure,
3,
189-199.
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PDB codes:
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D.Lassen,
C.Lücke,
M.Kveder,
A.Mesgarzadeh,
J.M.Schmidt,
B.Specht,
A.Lezius,
F.Spener,
and
H.Rüterjans
(1995).
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
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Eur J Biochem,
230,
266-280.
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PDB code:
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J.H.Veerkamp,
and
R.G.Maatman
(1995).
Cytoplasmic fatty acid-binding proteins: their structure and genes.
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Prog Lipid Res,
34,
17-52.
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L.X.Chen,
Z.P.Zhang,
A.Scafonas,
R.C.Cavalli,
J.L.Gabriel,
K.J.Soprano,
and
D.R.Soprano
(1995).
Arginine 132 of cellular retinoic acid-binding protein (type II) is important for binding of retinoic acid.
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J Biol Chem,
270,
4518-4525.
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A.C.Young,
G.Scapin,
A.Kromminga,
S.B.Patel,
J.H.Veerkamp,
and
J.C.Sacchettini
(1994).
Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids.
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Structure,
2,
523-534.
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PDB codes:
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E.Schievano,
D.Quarzago,
P.Spadon,
H.L.Monaco,
G.Zanotti,
and
E.Peggion
(1994).
Conformational and binding properties of chicken liver basic fatty acid binding protein in solution.
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Biopolymers,
34,
879-887.
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G.J.Kleywegt,
T.Bergfors,
H.Senn,
P.Le Motte,
B.Gsell,
K.Shudo,
and
T.A.Jones
(1994).
Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid.
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Structure,
2,
1241-1258.
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PDB codes:
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D.Ricquier,
and
A.M.Cassard-Doulcier
(1993).
The biochemistry of white and brown adipocytes analysed from a selection of proteins.
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Eur J Biochem,
218,
785-796.
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G.Scapin,
A.C.Young,
A.Kromminga,
J.H.Veerkamp,
J.I.Gordon,
and
J.C.Sacchettini
(1993).
High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid: protein interactions.
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Mol Cell Biochem,
123,
3.
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T.Börchers,
and
F.Spener
(1993).
Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver.
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Mol Cell Biochem,
123,
23-27.
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M.Sheridan,
and
D.C.Wilton
(1992).
The binding of the fluorescent ATP analogue 2'(3')-trinitrophenyladenosine-5'-triphosphate to rat liver fatty acid-binding protein.
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FEBS Lett,
314,
486-488.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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