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PDBsum entry 1blr
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* Residue conservation analysis
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DOI no:
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Biochemistry
37:12727-12736
(1998)
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PubMed id:
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NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
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L.Wang,
Y.Li,
F.Abildgaard,
J.L.Markley,
H.Yan.
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ABSTRACT
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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.
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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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X.Zhou,
Y.Lu,
W.Wang,
B.Borhan,
and
G.E.Reid
(2010).
'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.
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J Am Soc Mass Spectrom,
21,
1339-1351.
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K.S.Sandhu,
and
D.Dash
(2007).
Dynamic alpha-helices: conformations that do not conform.
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Proteins,
68,
109-122.
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I.Söderhäll,
A.Tangprasittipap,
H.Liu,
K.Sritunyalucksana,
P.Prasertsan,
P.Jiravanichpaisal,
and
K.Söderhäll
(2006).
Characterization of a hemocyte intracellular fatty acid-binding protein from crayfish (Pacifastacus leniusculus) and shrimp (Penaeus monodon).
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FEBS J,
273,
2902-2912.
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H.Xiao,
and
I.A.Kaltashov
(2005).
Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I.
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J Am Soc Mass Spectrom,
16,
869-879.
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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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L.Franzoni,
C.Lücke,
C.Pérez,
D.Cavazzini,
M.Rademacher,
C.Ludwig,
A.Spisni,
G.L.Rossi,
and
H.Rüterjans
(2002).
Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.
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J Biol Chem,
277,
21983-21997.
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PDB codes:
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B.Xiao,
G.Shi,
J.Gao,
J.Blaszczyk,
Q.Liu,
X.Ji,
and
H.Yan
(2001).
Unusual conformational changes in 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as revealed by X-ray crystallography and NMR.
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J Biol Chem,
276,
40274-40281.
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PDB codes:
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L.L.Burns,
and
I.J.Ropson
(2001).
Folding of intracellular retinol and retinoic acid binding proteins.
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Proteins,
43,
292-302.
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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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V.V.Krishnan,
M.Sukumar,
L.M.Gierasch,
and
M.Cosman
(2000).
Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding.
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Biochemistry,
39,
9119-9129.
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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
codes are
shown on the right.
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Links
