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PDBsum entry 1lft
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Oxygen storage/transport
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PDB id
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1lft
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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 human oxy- And deoxyhaemoglobin at different levels of humidity: variability in the t state.
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Authors
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B.K.Biswal,
M.Vijayan.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
1155-1161.
[DOI no: ]
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PubMed id
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Abstract
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High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at
different levels of environmental humidity and solvent content. The structure of
the oxy form remains relatively unchanged at all levels. The deoxy form,
however, undergoes a water-mediated transformation when the relative humidity
around the crystals is reduced below 93%. The space group is maintained during
the transformation, but the unit-cell volume nearly doubles, with two tetrameric
molecules in the asymmetric unit of the low-humidity form compared with one in
the native crystals. Interestingly, the haem geometry in the low-humidity form
is closer to that in the oxy form than to that in the native deoxy form. The
quaternary structure of one of the tetramers moves slightly towards that in the
oxy form, while that in the other is more different from the oxy form than that
in the high-salt native deoxy form. Thus, it would appear that, as in the case
of the liganded form, the deoxy form of haemoglobin can also access an ensemble
of related T states.
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Figure 3.
Figure 3 The relationship between the unit cells of the native
and the low-humidity form of deoxyhaemoglobin. The primed
symbols correspond to the low-humidity form.
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Figure 4.
Figure 4 Haem environment of the  -subunit
of native deoxy (red), molecule 1 of deoxy 90% r.h. (blue) and
oxy (green) structures.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2002,
58,
1155-1161)
copyright 2002.
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Secondary reference #1
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Title
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Structure of human oxyhaemoglobin at 2.1 a resolution.
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Author
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B.Shaanan.
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Ref.
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J Mol Biol, 1983,
171,
31-59.
[DOI no: ]
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PubMed id
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Figure 11.
FIG. 11. Plot the hange in non-bonded energy during rotation of Cys93fl about the C,-Cp bond.
Positive values ~b correspond to a clockwse rotation looking along the Cp--C~ bond, the observed
position being at ~b =0. -O-O, The calculation from which the nonbondd interaction with
Tyr145fl was excluded. The well at ~b ffi 120 ~ corresponds to the external position of Cys93fl (i.e. the
Hb-like conformation; see the text).
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Figure 13.
Fro. 13. h same region as displayed in Fig. 12 but in the fl subunit. The hydrogen bonds Oy(5)--
O(H19) and OH(HC2)--O(FGS) are shown by broken lines.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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The crystal structure of human deoxyhaemoglobin at 1.74 a resolution.
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Authors
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G.Fermi,
M.F.Perutz,
B.Shaanan,
R.Fourme.
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Ref.
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J Mol Biol, 1984,
175,
159-174.
[DOI no: ]
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PubMed id
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Figure 1.
FG2, FG4 /I1
CD2, CD3, FG2, FG4, haem fi,
CD5, CD8, D7, El-E3 a,
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Figure 3.
I'he 3.4 (4)
111: I'
1%~ > 44
3.x (4)
His 3.2 (9) 1: K Hi,
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #3
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Title
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A third quaternary structure of human hemoglobin a at 1.7-A resolution.
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Authors
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M.M.Silva,
P.H.Rogers,
A.Arnone.
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Ref.
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J Biol Chem, 1992,
267,
17248-17256.
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PubMed id
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