 |
PDBsum entry 1blr
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Nmr solution structure of type ii human cellular retinoic acid binding protein: implications for ligand binding.
|
|
|
Authors
|
|
L.Wang,
Y.Li,
F.Abildgaard,
J.L.Markley,
H.Yan.
|
|
|
Ref.
|
|
Biochemistry, 1998,
37,
12727-12736.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The structure of human apo-cellular retinoic acid binding protein II
(apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The
sequential assignments of the 1H, 13C, and 15N resonances of apo-CRABPII were
established by multinuclear, multidimensional NMR spectroscopy. The solution
structure of apo-CRABPII was derived from 2382 experimental NMR restraints using
a hybrid distance geometry-simulated annealing protocol. The root-mean-square
deviation of the ensemble of 25 refined conformers that represent the structure
from the mean coordinate set derived from them was 0.54 +/- 0.18 and 0.92 +/-
0.20 A for the backbone atoms and all heavy atoms, respectively, of all residues
except Ala32-Pro39 and Thr57-Glu62, which are in disordered regions. The
solution structure of apo-CRABPII is similar to the crystal structure of
holo-CRABPII [Kleywegt, G. J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B.,
Shudo, K., and Jones, T. A. (1994) Structure 2, 1241-1258] except the ligand
entrance, which is sufficiently enlarged in the apoprotein to be readily
accessible to retinoic acid. The enlargement of the ligand entrance of
apo-CRABPII relative to that of holo-CRABPII is due mainly to a concerted
conformational change in three structural elements, namely, the second helix,
the betaC-betaD loop, and the betaE-betaF loop. Furthermore, the ligand-binding
pocket of apo-CRABPII showed evidence of dynamic disorder; among the 21 residues
that constitute this pocket, 16 residues had weak or no detectable cross-peaks
in the two-dimensional 1H-15N HSQC spectrum recorded under conditions of minimal
water saturation or dephasing. Apo-CRABPII is largely monomeric in solution,
with no evidence for the dimeric structure shown in the crystal structure of
apo-CRABPI which was suggested to be a prerequisite for ligand entry [Thompson,
J. R., Bratt, J. M., and Banaszak, L. J. (1995) J. Mol. Biol. 252, 433-446].
Thus, the widening of the ligand entrance required for entry of retinoic acid
appears to be a property of monomeric apo-CRABPII.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystal structures of cellular retinoic acid binding proteins i and ii in complex with all-Trans-Retinoic acid and a synthetic retinoid.
|
|
|
Authors
|
|
G.J.Kleywegt,
T.Bergfors,
H.Senn,
P.Le motte,
B.Gsell,
K.Shudo,
T.A.Jones.
|
|
|
Ref.
|
|
Structure, 1994,
2,
1241-1258.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
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).
|
|
|
|
|
|
The above figure is
reproduced from the cited reference
with permission from Cell Press
|
|
|
|
|
|
|
