1r1y

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{{STRUCTURE_1r1y| PDB=1r1y | SCENE= }}
{{STRUCTURE_1r1y| PDB=1r1y | SCENE= }}
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'''Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom'''
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===Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom===
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==Overview==
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Hemoglobin (Hb) Bassett, an abnormal Hb variant with a markedly reduced oxygen affinity, was discovered in a Caucasian (Anglo-Saxon) male child who experienced episodes of cyanosis. Cation-exchange and reversed-phase (RP) high-performance liquid chromatography (HPLC) showed that the patient has an abnormal Hb, with a mutation in the alpha-globin. Tryptic peptide digest of the abnormal alpha-globin with subsequent HPLC analysis revealed abnormal elution of the alpha-T11 peptide. Further studies with Edman sequencing and electrospray mass spectrometry of tryptic peptide alpha-T11, as well as structural analysis by X-ray crystallography revealed an Asp--&gt;Ala substitution at the alpha94 (G1) position, a match for Hb Bassett. Detailed functional studies showed that this Hb variant had a markedly reduced oxygen affinity (P(50) at pH 7.0 = 22 mmHg; Hb A P(50) = 10.5 mmHg), reduced Bohr effect (-0.26 compared to - 0.54 in Hb A), and low subunit cooperativity (n = 1.4, compared to 2.6 in Hb A). X-ray crystallography results explain the probable effects of the structural modification on the oxygen-binding properties of this Hb variant.
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{{ABSTRACT_PUBMED_15495251}}
==About this Structure==
==About this Structure==
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[[Category: Oxygen affinity]]
[[Category: Oxygen affinity]]
[[Category: Rochester]]
[[Category: Rochester]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:41:15 2008''

Revision as of 22:41, 28 July 2008

Template:STRUCTURE 1r1y

Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom

Template:ABSTRACT PUBMED 15495251

About this Structure

1R1Y is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity., Abdulmalik O, Safo MK, Lerner NB, Ochotorena J, Daikhin E, Lakka V, Santacroce R, Abraham DJ, Asakura T, Am J Hematol. 2004 Nov;77(3):268-76. PMID:15495251

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