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| - | [[Image:1qi8.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1qi8| PDB=1qi8 | SCENE= }} | | {{STRUCTURE_1qi8| PDB=1qi8 | SCENE= }} |
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| - | '''DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT'''
| + | ===DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT=== |
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| - | ==Overview==
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| - | Functional and structural studies on hemoglobin and myoglobin from different animals and engineered variants have enlightened the great importance of the physico-chemical properties of the side-chains at topological position B10 and E7. These residues proved to be crucial to the discrimination and stabilisation of gaseous ligands. In view of the data obtained on the high oxygen affinity hemoglobin from Ascaris worms and a new mutant of sperm whale myoglobin, we selected the two mutations Leu B10-->Tyr and His E7-->Gln as potentially relevant to control ligand binding parameters in the alpha and beta-chains of human hemoglobin. Here, we present an investigation of three new mutants: HbalphaYQ (alpha2YQbeta2A), HbbetaYQ (alpha2Abeta2YQ) and HbalphabetaYQ (alpha2YQbeta2YQ). They are characterised by a very low reactivity for NO, O2 and CO, and a reduced cooperativity. Their functional properties are not inconsistent with the behaviour expected for a two-state allosteric model. Proteins with these substitutions may be considered as candidates for the synthesis of a possible "blood substitute", which should yield an O2 adduct stable to autoxidation and slowly reacting with NO. The mutant HbalphabetaYQ is particularly interesting because the rate of reaction of NO with the oxy and deoxy derivatives is reduced. A structural interpretation of our data is presented based on the 3D structure of deoxy HbalphabetaYQ determined by crystallography at 1.8 A resolution.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10390349}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10390349 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10390349}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hemoglobin]] | | [[Category: Hemoglobin]] |
| | [[Category: Low no reactivity]] | | [[Category: Low no reactivity]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:18:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:29:15 2008'' |
Revision as of 23:29, 27 July 2008
Template:STRUCTURE 1qi8
DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT
Template:ABSTRACT PUBMED 10390349
About this Structure
1QI8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Modulation of ligand binding in engineered human hemoglobin distal pocket., Miele AE, Santanche S, Travaglini-Allocatelli C, Vallone B, Brunori M, Bellelli A, J Mol Biol. 1999 Jul 9;290(2):515-24. PMID:10390349
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