PittsburghV1, Main, Exploration, bibRecord, 000021

A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.

Identifieur interne : 000021 ( Main/Exploration ); précédent : 000020; suivant : 000022

A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.

Auteurs : Matthew J. Whitley [États-Unis] ; Zhaoyong Xi [États-Unis] ; Jonathan C. Bartko [États-Unis] ; Malene Ringkj Bing Jensen [France] ; Martin Blackledge [France] ; Angela M. Gronenborn [États-Unis]

Source :

Biophysical Journal [ 0006-3495 ] ; 2017-03-28.

RBID : Hal:hal-01538732

Abstract

A cataract is a pathological condition characterized by the clouding of the normally clear eye lens brought about by deposition of crystallin proteins in the lens fiber cells. These protein aggregates reduce visual acuity by scattering or blocking incoming light. Chemical damage to proteins of the crystallin family, accumulated over a lifetime, leads to age-related cataract, whereas inherited mutations are associated with congenital or early-onset cataract. The V75D mutant of γD-crystallin is associated with congenital cataract in mice and was previously shown to un/fold via a partially folded intermediate. Here, we structurally characterized the stable equilibrium urea unfolding intermediate of V75D at the ensemble level using solution NMR and small-angle x-ray scattering. Our data show that, in the intermediate, the C-terminal domain retains a folded conformation that is similar to the native wild-type protein, whereas the N-terminal domain is unfolded and comprises an ensemble of random conformers, without any detectable residual structural propensities.

Url:

https://hal.archives-ouvertes.fr/hal-01538732

DOI: 10.1016/j.bpj.2017.02.010

Affiliations:

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

to stream Hal, to step Corpus: 000012
to stream Hal, to step Curation: 000012
to stream Hal, to step Checkpoint: 000021
to stream Main, to step Merge: 000021
to stream Main, to step Curation: 000021

Le document en format XML

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          <orgName>Université Joseph Fourier - Grenoble 1</orgName>
          <orgName type="acronym">UJF</orgName>
          <date type="end">2015-12-31</date>
          <desc>            <address>              <addrLine>BP 53 - 38041 Grenoble Cedex 9</addrLine>
              <country key="FR"></country>
            </address>
            <ref type="url">http://www.ujf-grenoble.fr/</ref>
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</tutelle>
<tutelle name="DRF/IBS" active="#struct-300016" type="direct"><org type="institution" xml:id="struct-300016" status="VALID">          <orgName>Commissariat à l'énergie atomique et aux énergies alternatives</orgName>
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            </address>
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<tutelle name="UMR5075" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID">          <idno type="IdRef">02636817X</idno>
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          <date type="start">1939-10-19</date>
          <desc>            <address>              <country key="FR"></country>
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</tutelle>
<tutelle active="#struct-445543" type="direct"><org type="institution" xml:id="struct-445543" status="VALID"><idno type="IdRef">188399275</idno>
<orgName>Université Grenoble Alpes</orgName>
<orgName type="acronym">UGA</orgName>
<date type="start">2016-01-01</date>
<desc><address><addrLine>CS 40700 - 38058 Grenoble cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-grenoble-alpes.fr</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
<placeName><settlement type="city">Grenoble</settlement>
<region type="region" nuts="2">Auvergne-Rhône-Alpes</region>
<region type="old region" nuts="2">Rhône-Alpes</region>
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<orgName type="university">Université Joseph Fourier</orgName>
<orgName type="institution" wicri:auto="newGroup">Université de Grenoble</orgName>
<placeName><settlement type="city">Grenoble</settlement>
<region type="region" nuts="2">Auvergne-Rhône-Alpes</region>
<region type="old region" nuts="2">Rhône-Alpes</region>
</placeName>
<orgName type="university">Université Grenoble-Alpes</orgName>
</affiliation>
</author>
<author><name sortKey="Gronenborn, Angela M" sort="Gronenborn, Angela M" uniqKey="Gronenborn A" first="Angela M" last="Gronenborn">Angela M. Gronenborn</name>
<affiliation wicri:level="1"><hal:affiliation type="department" xml:id="struct-465999" status="INCOMING">          <orgName>Department of Structural Biology</orgName>
          <desc>            <address>              <addrLine>University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15260, United States</addrLine>
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            </address>
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          <desc>            <address>              <addrLine>4200 Fifth AvenuePittsburgh, PA 15260</addrLine>
              <country key="US"></country>
            </address>
            <ref type="url">http://www.pitt.edu/</ref>
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</hal:affiliation>
<country>États-Unis</country>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.1016/j.bpj.2017.02.010</idno>
<series><title level="j">Biophysical Journal</title>
<idno type="ISSN">0006-3495</idno>
<imprint><date type="datePub">2017-03-28</date>
</imprint>
</series>
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<front><div type="abstract" xml:lang="en">A cataract is a pathological condition characterized by the clouding of the normally clear eye lens brought about by deposition of crystallin proteins in the lens fiber cells. These protein aggregates reduce visual acuity by scattering or blocking incoming light. Chemical damage to proteins of the crystallin family, accumulated over a lifetime, leads to age-related cataract, whereas inherited mutations are associated with congenital or early-onset cataract. The V75D mutant of γD-crystallin is associated with congenital cataract in mice and was previously shown to un/fold via a partially folded intermediate. Here, we structurally characterized the stable equilibrium urea unfolding intermediate of V75D at the ensemble level using solution NMR and small-angle x-ray scattering. Our data show that, in the intermediate, the C-terminal domain retains a folded conformation that is similar to the native wild-type protein, whereas the N-terminal domain is unfolded and comprises an ensemble of random conformers, without any detectable residual structural propensities.</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
<li>États-Unis</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Grenoble</li>
</settlement>
<orgName><li>Université Grenoble-Alpes</li>
<li>Université Joseph Fourier</li>
<li>Université de Grenoble</li>
</orgName>
</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Whitley, Matthew J" sort="Whitley, Matthew J" uniqKey="Whitley M" first="Matthew J" last="Whitley">Matthew J. Whitley</name>
</noRegion>
<name sortKey="Bartko, Jonathan C" sort="Bartko, Jonathan C" uniqKey="Bartko J" first="Jonathan C" last="Bartko">Jonathan C. Bartko</name>
<name sortKey="Gronenborn, Angela M" sort="Gronenborn, Angela M" uniqKey="Gronenborn A" first="Angela M" last="Gronenborn">Angela M. Gronenborn</name>
<name sortKey="Xi, Zhaoyong" sort="Xi, Zhaoyong" uniqKey="Xi Z" first="Zhaoyong" last="Xi">Zhaoyong Xi</name>
</country>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Jensen, Malene Ringkj Bing" sort="Jensen, Malene Ringkj Bing" uniqKey="Jensen M" first="Malene Ringkj Bing" last="Jensen">Malene Ringkj Bing Jensen</name>
</region>
<name sortKey="Blackledge, Martin" sort="Blackledge, Martin" uniqKey="Blackledge M" first="Martin" last="Blackledge">Martin Blackledge</name>
</country>
</tree>
</affiliations>
</record>

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A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.

A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.

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