1nqp
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(New page: 200px<br /> <applet load="1nqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nqp, resolution 1.73Å" /> '''Crystal structure o...)
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Revision as of 11:08, 8 November 2007
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Crystal structure of Human hemoglobin E at 1.73 A resolution
Overview
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.
About this Structure
1NQP is a Protein complex structure of sequences from Homo sapiens with CYN and HEM as ligands. Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary X-ray structural studies of hemoglobin A2 and hemoglobin E, isolated from the blood samples of beta-thalassemic patients., Dasgupta J, Sen U, Choudhury D, Datta P, Chakrabarti A, Chakrabarty SB, Chakrabarty A, Dattagupta JK, Biochem Biophys Res Commun. 2003 Apr 4;303(2):619-23. PMID:12659864
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