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| {{STRUCTURE_1r1x| PDB=1r1x | SCENE= }} | | {{STRUCTURE_1r1x| PDB=1r1x | SCENE= }} |
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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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| ==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-->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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15495251}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15495251 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15495251}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxygen affinity]] | | [[Category: Oxygen affinity]] |
| [[Category: Rochester]] | | [[Category: Rochester]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:58:33 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:06:03 2008'' |