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PDBsum entry 2cbs
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Transport protein
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PDB id
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2cbs
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structures of cellular retinoic acid binding proteins i and ii in complex with synthetic retinoids.
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Authors
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B.N.Chaudhuri,
G.J.Kleywegt,
I.Broutin-L'Hermite,
T.Bergfors,
H.Senn,
P.Le motte,
O.Partouche,
T.A.Jones.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1850-1857.
[DOI no: ]
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PubMed id
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Abstract
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Retinoids play important roles in diverse cellular processes including growth,
cell differentiation and vision. Many natural and synthetic retinoids are used
as drugs in dermatology and oncology. A large amount of data has been
accumulated on the cellular activity of different synthetic retinoids. They are
stabilized and transported inside the cell cytoplasm by binding and transport
proteins, such as cellular retinol-binding proteins and cellular retinoic acid
binding proteins (CRABPs). The structures of human CRABP II in complex with two
different synthetic retinoids, Ro13-6307 and Ro12--7310 (at 2.1 and 2.0 A
resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic
acid, Am80 (at 2.8 A resolution) are described. The binding affinities of human
CRABP I and II for the retinoids studied here have been determined. All these
compounds have comparable binding affinities (nanomolar range) for both CRABPs.
Apart from the particular interactions of the carboxylate group of the retinoids
with specific protein groups, each structure reveals characteristic
interactions. Studying the atomic details of the interaction of retinoids with
retinoid-binding proteins facilitates the understanding of the kinetics of
retinoid trafficking inside the cytoplasm.
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Figure 1.
Figure 1 C^  trace
of CRABP II in complex with retinoic acid (PDB code 1cbs).
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Figure 6.
Figure 6 The interaction of Am80 with CRABP I (yellow C atoms;
red O atoms; blue N atoms).  [A]-weighted
simulated-annealing omit density for the ligand (Read,
1986[Read, R. J. (1986). Acta Cryst. A42, 140-149.]; Hodel et
al., 1992[Hodel, A., Kim, S.-H. & Brünger, A. T. (1992). Acta
Cryst. A48, 851-858.]) is shown. Hydrogen-bonding interactions
are indicated by dashed lines.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1999,
55,
1850-1857)
copyright 1999.
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Secondary reference #1
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Title
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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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Authors
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G.J.Kleywegt,
T.Bergfors,
H.Senn,
P.Le motte,
B.Gsell,
K.Shudo,
T.A.Jones.
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Ref.
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Structure, 1994,
2,
1241-1258.
[DOI no: ]
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PubMed id
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Figure 8.
Figure 8. Comparison of retinoid binding in CRABP II and
CRBP I. The Ca trace, RA and side-chain atoms of Arg111, Arg132
and Tyr134 of CRABP II have been coloured as in Figure 7, and
the solvent-accessible surface of CRABP II has been drawn in
purple. For CRBP I, the retinol has been coloured green, its
solvent-accessible surface red, and the side-chain atoms of
Gln108, Gln128 and Phe130 have been coloured green (carbon),
cyan (nitrogen) and pink (oxygen).
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #2
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Title
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Lipid-Binding proteins: a family of fatty acid and retinoid transport proteins.
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Authors
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L.Banaszak,
N.Winter,
Z.Xu,
D.A.Bernlohr,
S.Cowan,
T.A.Jones.
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Ref.
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Adv Protein Chem, 1994,
45,
89.
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PubMed id
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Secondary reference #3
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Title
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Crystallization and preliminary X-Ray analysis of recombinant bovine cellular retinoic acid-Binding protein.
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Authors
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T.Bergfors,
G.J.Kleywegt,
T.A.Jones.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1994,
50,
370-374.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Retinoic acid absorbs at 350 nm. The protein-retinoic acid
spectrum can be evaluated by the ratio ,435028o. For protein
fully saturated with retinoic acid, this ratio is 2.07. When
protected from the light, the complex is stable for at least 7
months and this value remains essentially unchanged. When
exposed to light, deterioration beg'.ms within 30 min, as moni-
tored by a decrease in the absorbarice of retinoic acid at A350.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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