1r1x

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[[Image:1r1x.gif|left|200px]]
[[Image:1r1x.gif|left|200px]]
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{{Structure
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|PDB= 1r1x |SIZE=350|CAPTION= <scene name='initialview01'>1r1x</scene>, resolution 2.15&Aring;
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The line below this paragraph, containing "STRUCTURE_1r1x", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MBN:TOLUENE'>MBN</scene>
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{{STRUCTURE_1r1x| PDB=1r1x | SCENE= }}
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|RELATEDENTRY=[[1r1y|1R1Y]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1x OCA], [http://www.ebi.ac.uk/pdbsum/1r1x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r1x RCSB]</span>
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'''Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom'''
'''Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom'''
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[[Category: Ochotorena, J.]]
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[[Category: Safo, M K.]]
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[[Category: carbon monoxide]]
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[[Category: Carbon monoxide]]
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[[Category: Crystal structure]]
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[[Category: hemoglobin]]
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[[Category: Hemoglobin]]
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[[Category: mutant]]
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[[Category: Mutant]]
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[[Category: oxygen affinity]]
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[[Category: Oxygen affinity]]
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[[Category: rochester]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:58:33 2008''
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Revision as of 03:58, 3 May 2008

Template:STRUCTURE 1r1x

Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom


Overview

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-->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.

About this Structure

1R1X 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 Page seeded by OCA on Sat May 3 06:58:33 2008

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