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PDBsum entry 1dxt
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Oxygen transport
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PDB id
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1dxt
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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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High-Resolution X-Ray study of deoxy recombinant human hemoglobins synthesized from beta-Globins having mutated amino termini.
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Authors
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J.S.Kavanaugh,
P.H.Rogers,
A.Arnone.
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Ref.
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Biochemistry, 1992,
31,
8640-8647.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structures of three mutant hemoglobins reconstituted from
recombinant beta chains and authentic human alpha chains have been determined in
the deoxy state at 1.8-A resolution. The primary structures of the mutant
hemoglobins differ at the beta-chain amino terminus. One mutant, beta Met, is
characterized by the addition of a methionine at the amino terminus. The other
two hemoglobins are characterized by substitution of Val 1 beta with either a
methionine, beta V1M, or an alanine, beta V1A. All the mutation-induced
structural perturbations are small intrasubunit changes that are localized to
the immediate vicinity of the beta-chain amino terminus. In the beta Met and
beta V1A mutants, the mobility of the beta-chain amino terminus increases and
the electron density of an associated inorganic anion is decreased. In contrast,
the beta-chain amino terminus of the beta V1M mutant becomes less mobile, and
the inorganic anion binds with increased affinity. These structural differences
can be correlated with functional data for the mutant hemoglobins [Doyle, M. L.,
Lew, G., DeYoung, A., Kwiatkowski, L., Noble, R. W., & Ackers, G. K. (1992)
Biochemistry preceding paper is this issue] as well as with the properties of
ruminant hemoglobins and a mechanism [Perutz, M., & Imai, K. (1980) J. Mol.
Biol. 136, 183-191] that relates the intrasubunit interactions of the beta-chain
amino terminus to changes in oxygen affinity. Since the structures of the mutant
deoxyhemoglobins show only subtle differences from the structure of
deoxyhemoglobin A, it is concluded that any of the three hemoglobins could
probably function as a surrogate for hemoglobin A.(ABSTRACT TRUNCATED AT 250
WORDS)
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Secondary reference #1
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Title
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Functional properties of human hemoglobins synthesized from recombinant mutant beta-Globins.
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Authors
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M.L.Doyle,
G.Lew,
A.De young,
L.Kwiatkowski,
A.Wierzba,
R.W.Noble,
G.K.Ackers.
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Ref.
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Biochemistry, 1992,
31,
8629-8639.
[DOI no: ]
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PubMed id
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