PittsburghV1, France, Analysis, bibRecord, 000045

Modulation of hemoglobin dynamics by an allosteric effector

Identifieur interne : 000045 ( France/Analysis ); précédent : 000044; suivant : 000046

Modulation of hemoglobin dynamics by an allosteric effector

Auteurs : Jyotsana Lal [États-Unis] ; Marco Maccarini [France] ; Peter Fouquet [France] ; Nancy Ho [États-Unis] ; Chien Ho [États-Unis] ; Lee Makowski [États-Unis]

Source :

Protein Science [ 0961-8368 ] ; 2016-12-15.

RBID : Hal:hal-01538121

English descriptors

mix :
- X-ray solution scattering, hemoglobin, neutron spin echo, protein dynamics.

Abstract

Hemoglobin (Hb) is an extensively studied paradigm of proteins that alter their function in response to allosteric effectors. Models of its action have been used as prototypes for structure-function relationships in many proteins, and models for the molecular basis of its function have been deeply studied and extensively argued. Recent reports suggest that dynamics may play an important role in its function. Relatively little is known about the slow, correlated motions of hemo-globin subunits in various structural states because experimental and computational strategies for their characterization are challenging. Allosteric effectors such as inositol hexaphosphate (IHP) bind to both deoxy-Hb and HbCO, albeit at different sites, leading to a lowered oxygen affinity. The manner in which these effectors impact oxygen binding is unclear and may involve changes in structure, dynamics or both. Here we use neutron spin echo measurements accompanied by wide-angle X-ray scattering to show that binding of IHP to HbCO results in an increase in the rate of coordinated motions of Hb subunits relative to one another with little if any change in large scale structure. This increase of large-scale dynamics seems to be coupled with a decrease in the average magnitude of higher frequency modes of individual residues. These observations indicate that enhanced dynamic motions contribute to the functional changes induced by IHP and suggest that they may be responsible for the lowered oxygen affinity triggered by these effectors.

Url:

https://hal.archives-ouvertes.fr/hal-01538121

DOI: 10.1002/pro.3099

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Main, to step Exploration: 000051
to stream France, to step Extraction: 000045

Links to Exploration step

Hal:hal-01538121

Le document en format XML

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<front><div type="abstract" xml:lang="en">Hemoglobin (Hb) is an extensively studied paradigm of proteins that alter their function in response to allosteric effectors. Models of its action have been used as prototypes for structure-function relationships in many proteins, and models for the molecular basis of its function have been deeply studied and extensively argued. Recent reports suggest that dynamics may play an important role in its function. Relatively little is known about the slow, correlated motions of hemo-globin subunits in various structural states because experimental and computational strategies for their characterization are challenging. Allosteric effectors such as inositol hexaphosphate (IHP) bind to both deoxy-Hb and HbCO, albeit at different sites, leading to a lowered oxygen affinity. The manner in which these effectors impact oxygen binding is unclear and may involve changes in structure, dynamics or both. Here we use neutron spin echo measurements accompanied by wide-angle X-ray scattering to show that binding of IHP to HbCO results in an increase in the rate of coordinated motions of Hb subunits relative to one another with little if any change in large scale structure. This increase of large-scale dynamics seems to be coupled with a decrease in the average magnitude of higher frequency modes of individual residues. These observations indicate that enhanced dynamic motions contribute to the functional changes induced by IHP and suggest that they may be responsible for the lowered oxygen affinity triggered by these effectors.</div>
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Modulation of hemoglobin dynamics by an allosteric effector

Modulation of hemoglobin dynamics by an allosteric effector

Source :

English descriptors

Abstract

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Links to Exploration step

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Pour manipuler ce document sous Unix (Dilib)

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