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PDBsum entry 2frs
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Transport protein
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PDB id
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2frs
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References listed in PDB file
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Key reference
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Title
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The structure of apo-Wild-Type cellular retinoic acid binding protein ii at 1.4 a and its relationship to ligand binding and nuclear translocation.
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Authors
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S.Vaezeslami,
E.Mathes,
C.Vasileiou,
B.Borhan,
J.H.Geiger.
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Ref.
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J Mol Biol, 2006,
363,
687-701.
[DOI no: ]
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PubMed id
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Abstract
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CRABPII is a small, cytosolic protein that solubilizes and transfers retinoic
acid (RA) to the nucleus while also enhancing its transcriptional activity. We
have determined the first high-resolution structure of apo-wild type (WT)
CRABPII at 1.35 A. Using three different data sets collected on apo-WT CRABPII
we have shown that apo- and holo-CRABPII share very similar structures. Binding
of RA appears to increase the overall rigidity of the structure, although the
induced structural changes are not as pronounced as previously thought. The
enhanced structural rigidity may be an important determinant for the enhanced
nuclear localization of the RA-bound protein. Comparison of our apo-WT with a
mutant apo-CRABPII structure shows that mutation of Arg111, a conserved residue
of CRABPII and a key residue in RA binding, causes structural changes in the
molecule. We further investigated the structural importance of conserved
residues by determining the structure of the F15W mutant CRABPII (F15W-CRABPII).
Our structures also demonstrate structural changes induced by crystal packing
and show that a crystal can harbor demonstrative structural differences in the
asymmetric unit.
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Figure 2.
Figure 2. Structural differences between the two molecules in
the asymmetric unit of apo-CRABPII. Superimposed structures of
Mol A (green) and Mol B (hot pink) of Xtal1. Figure 2.
Structural differences between the two molecules in the
asymmetric unit of apo-CRABPII. Superimposed structures of Mol A
(green) and Mol B (hot pink) of Xtal1.
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Figure 4.
Figure 4. The significant structural consequences of the R111M
mutation. (a) Mol A's of R111M (red) and Xtal1 (green); and (b)
Mol B's of R111M (blue) and Xtal1 (hot pink) are superimposed.
Figure 4. The significant structural consequences of the R111M
mutation. (a) Mol A's of R111M (red) and Xtal1 (green); and (b)
Mol B's of R111M (blue) and Xtal1 (hot pink) are superimposed.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2006,
363,
687-701)
copyright 2006.
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Secondary reference #1
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Title
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Determining crystal structures of proteins and protein complexes by x-Ray crystallography: x-Ray crystallographic studies of the mutants of cellular retinoic acid binding protein type ii toward designing a mimic of rhodopsin
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Author
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S.Vaezeslami.
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Ref.
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thesis ...
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