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PDBsum entry 1c7d
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Oxygen storage/transport
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PDB id
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1c7d
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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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Genetically crosslinked hemoglobin: a structural study.
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Author
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E.A.Brucker.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
812-816.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1
and rHb1.2, have been determined in the deoxy state at 1.8 A resolution. Two of
the three proteins, rHb1.1 and rHb1.2, contain a genetic fusion of the alpha
subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The
glycine crosslinks, localized between one N- and C--termini pair of the alpha
subunits in the deoxy crystalline state, do not perturb the overall tertiary or
quaternary or even the local structure of hemoglobin. Therefore, genetic fusion
to prevent the dissociation of the hemoglobin tetramer, thereby inhibiting renal
clearance based upon molecular size, is a structurally conservative method to
stabilize hemoglobin for use as an oxygen-delivery therapeutic.
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Figure 2.
Figure 2 Overlay of HbA[0], rHb1.1 and rHb1.2. Stereoview
includes the  subunit
N- and C-termini (glycine crosslink) region; HbA[0] (Protein
Data Bank entry 2hhb; Fermi et al., 1984[Fermi, G., Perutz, M.
F., Shaanan, B. & Fourme, R. (1984). J. Mol. Biol. 175,
159-174.]) with associated text is drawn in black, rHb1.1 in
light gray and rHb1.2 in dark gray. Coordinates were superposed
by overlaying the C^ atoms
of the hemoglobins.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2000,
56,
812-816)
copyright 2000.
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Secondary reference #1
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Title
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Structures of a hemoglobin-Based blood substitute: insights into the function of allosteric proteins.
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Authors
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K.S.Kroeger,
C.E.Kundrot.
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Ref.
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Structure, 1997,
5,
227-237.
[DOI no: ]
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PubMed id
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Figure 5.
Figure 5. The glycine-bridge region. (a) Section of the
deoxy-rHb 1.1 electron-density map showing the glycine-bridge
region of the di-a-chain. (b) Section of the cyanomet-rHb 1.1
electron-density map showing the glycine bridge region of the
di-a-chain. Residues Arga141, Glya142, and Vala143 are shown.
The maps are contoured at 0.75s using coefficients (2F[o] -F[c])
and phases from the final models. The atoms are colored by atom
type (yellow, carbon; red, oxygen; blue, nitrogen).
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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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A human recombinant haemoglobin designed for use as a blood substitute.
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Authors
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D.Looker,
D.Abbott-Brown,
P.Cozart,
S.Durfee,
S.Hoffman,
A.J.Mathews,
J.Miller-Roehrich,
S.Shoemaker,
S.Trimble,
G.Fermi.
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Ref.
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Nature, 1992,
356,
258-260.
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PubMed id
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