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PDBsum entry 1nqp
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Oxygen storage/transport
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PDB id
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1nqp
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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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Crystallization and preliminary X-Ray structural studies of hemoglobin a2 and hemoglobin e, Isolated from the blood samples of beta-Thalassemic patients.
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Authors
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J.Dasgupta,
U.Sen,
D.Choudhury,
P.Datta,
A.Chakrabarti,
S.B.Chakrabarty,
A.Chakrabarty,
J.K.Dattagupta.
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Ref.
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Biochem Biophys Res Commun, 2003,
303,
619-623.
[DOI no: ]
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PubMed id
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Abstract
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Hemoglobin A(2) (alpha(2)delta(2)), a minor (2-3%) component of circulating red
blood cells, acts as an anti-sickling agent and its elevated concentration in
beta-thalassemia is a useful clinical diagnostic. In beta-thalassemia major,
where there is a failure of beta-chain production, HbA(2) acts as the
predominant oxygen delivery mechanism. Hemoglobin E, is another common abnormal
hemoglobin, caused by splice site mutation in exon 1 of beta globin gene, when
combines with beta-thalassemia, causes severe microcytic anemia. The
purification, crystallization, and preliminary structural studies of HbA(2) and
HbE are reported here. HbA(2) and HbE are purified by cation exchange column
chromatography in presence of KCN from the blood samples of individuals
suffering from beta-thalassemia minor and E beta-thalassemia. X-ray diffraction
data of HbA(2) and HbE were collected upto 2.1 and 1.73 A, respectively. HbA(2)
crystallized in space group P2(1) with unit cell parameters a=54.33 A, b=83.73
A, c=62.87 A, and beta=99.80 degrees whereas HbE crystallized in space group
P2(1)2(1)2(1) with unit cell parameters a=60.89 A, b=95.81 A, and c=99.08 A.
Asymmetric unit in each case contains one Hb tetramer in R(2) state.
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