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Restoring allosterism with compensatory mutations in hemoglobin.

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Restoring allosterism with compensatory mutations in hemoglobin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ho, N. T. Kim, H. W. Madrid, M. Tam, M. F. Zou, M. Shen, T. J. Ho, C. Sun, D. P. Cottam, P. F.
Description	Author Affiliation: Kim HW ( Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213.);
Abstract	Abnormal human hemoglobins (HBs) with amino acid substitutions in the alpha 1 beta 2 interface have very high oxygen affinity and greatly reduced cooperativity in O2 binding compared to normal human Hb. In such abnormal Hbs with mutations at position beta 99, the intersubunit hydrogen bonds between Asp-beta 99 and Tyr-alpha 42 and between Asp-beta 99 and Asn-alpha 97 are broken, thus destabilizing the deoxyquaternary structure of these Hbs. A molecular dynamics method has been used to design compensatory amino acid substitutions in these Hbs that can restore their allosteric properties. We have designed a compensatory mutation in a naturally occurring mutant Hb, Hb Kempsey (Asp-beta 99-->Asn), and have produced it using our Escherichia coli expression plasmid pHE2. We have determined the O2 binding properties of this recombinant double mutant Hb, Hb(Asp-beta 99-->Asn and Tyr-alpha 42-->Asp) and have used 1H NMR spectroscopy to investigate the tertiary structures around the heme groups and the quaternary structure in the alpha 1 beta 2 subunit interface. Our results clearly show that the Tyr-alpha 42-->Asp replacement can substantially compensate for the functional defect of Hb Kempsey caused by the Asp-beta 99-->Asn substitution. The structural and functional information derived from this recombinant Hb provides insights into the structural basis of allosterism and the design of compensatory amino acid substitutions to restore the functional properties of other abnormal HBs associated with hemoglobinopathies.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Allosteric Regulation Hemoglobins Chemistry Computer Simulation DNA Primers Globins Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Oxyhemoglobins Protein Conformation Structure-Activity Relationship Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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