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Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector.

Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Research Abstract Details 

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  • Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Abstract Text:

    sarata c sahuSarata C Sahu,virgil simplaceanuVirgil Simplaceanu,qingguo gongQingguo Gong,nancy t hoNancy T Ho,fang tianFang Tian,james h prestegardJames H Prestegard,chien hoChien Ho,

    We present a nuclear magnetic resonance (NMR) study in solution of the structures of human normal hemoglobin (Hb A) in the deoxy or unligated form in the absence and presence of an allosteric effector, inositol hexaphosphate (IHP), using 15N-1H residual dipolar coupling (RDC) measurements. There are several published crystal structures for deoxyhemoglobin A (deoxy-Hb A), and it has been reported that the functional properties of Hb A in single crystals are different from those in solution. Carbonmonoxyhemoglobin A (HbCO A) can also be crystallized in several structures. Our recent RDC studies of HbCO A in the absence and presence of IHP have shown that the solution structure of this Hb molecule is distinctly different from its classical crystal structures (R and R2). To have a better understanding of the structure-function relationship of Hb A under physiological conditions, we need to evaluate its structures in both ligated and unligated states in solution. Here, the intrinsic paramagnetic property of deoxy-Hb A has been exploited for the measurement of RDCs using the magnetic-field dependence of the apparent one-bond 1H-15N J couplings. Our RDC analysis suggests that the quaternary and tertiary structures of deoxy-Hb A in solution differ from its recently determined high-resolution crystal structures. Upon binding of IHP, structural changes in deoxy-Hb A are also observed, and these changes are largely within the alpha1beta1 (or alpha2beta2) dimer itself. These new structural findings allow us to gain a deeper insight into the structure-function relationship of this interesting allosteric protein.

    Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Publishing Authors By Initials

    sc sahuSC Sahu,v simplaceanuV Simplaceanu,q gongQ Gong,nt hoNT Ho,f tianF Tian,jh prestegardJH Prestegard,c hoC Ho,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

    PUBMED ID PMID:

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    Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Biochemistry

    VOLUME: 46

    Page Numbers: 9973-80

    Journal Abbreviation: Biochemistry

    ISSN: 0006-2960

    DAY: 11

    MONTH: 08

    YEAR: 2007

    Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370623

    Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Keywords Mesh Terms:

    KEYWORDS: Structure-Activity Relationship

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Information

    Substance Name: Hemoglobin A

    Registry Number: 9034-51-9

    Grant and Affiliation Information for Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector.

    AFFILIATION: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCRR

    GRANT: S10RR-017815

    ACRONYM: RR

    MEDLINETA: Biochemistry

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