Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein.
Identifieur interne : 000253 ( France/Analysis ); précédent : 000252; suivant : 000254Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein.
Auteurs : Malene Ringkj Bing Jensen [Norvège] ; Klaartje Houben ; Ewen Lescop [France] ; Laurence Blanchard [France] ; Rob W H. Ruigrok [France] ; Martin Blackledge [France]Source :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2008-06-25.
Abstract
A significant fraction of proteins coded in the human proteome do not fold into stable three-dimensional structures but are either partially or completely unfolded. A key feature of this family of proteins is their proposed capacity to undergo a disorder-to-order transition upon interaction with a physiological partner. The mechanisms governing protein folding upon interaction, in particular the extent to which recognition elements are preconfigured prior to formation of molecular complexes, can prove difficult to resolve in highly flexible systems. Here, we develop a conformational model of this type of protein, using an explicit description of the unfolded state, specifically modified to allow for the presence of transient secondary structure, and combining this with extensive measurement of residual dipolar couplings throughout the chain. This combination of techniques allows us to quantitatively analyze the level and nature of helical sampling present in the interaction site of the partially folded C-terminal domain of Sendai virus nucleoprotein (N(TAIL)). Rather than fraying randomly, the molecular recognition element of N(TAIL) preferentially populates three specific overlapping helical conformers, each stabilized by an N-capping interaction. The unfolded strands adjacent to the helix are thereby projected in the direction of the partner protein, identifying a mechanism by which they could achieve nonspecific encounter interactions prior to binding. This study provides experimental evidence for the molecular basis of helix formation in partially folded peptide chains, carrying clear implications for understanding early steps of protein folding.
Url:
DOI: 10.1021/ja801332d
Affiliations:
- France, Norvège
- Auvergne-Rhône-Alpes, Rhône-Alpes
- Lyon
- Université Claude Bernard Lyon 1, Université de Lyon
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Links to Exploration step
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<orgName type="acronym">UCBL</orgName>
<desc> <address> <addrLine>43, boulevard du 11 novembre 1918, 69622 Villeurbanne cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-lyon1.fr/</ref>
</desc>
<listRelation> <relation active="#struct-301088" type="direct"></relation>
</listRelation>
</org>
</tutelle>
<tutelle active="#struct-301088" type="indirect"><org type="regroupinstitution" xml:id="struct-301088" status="VALID"> <orgName>Université de Lyon</orgName>
<desc> <address> <addrLine>92 rue Pasteur - CS 30122, 69361 Lyon Cedex 07</addrLine>
<country key="FR"></country>
</address>
<ref type="url">https://www.universite-lyon.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR5086" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
<placeName><settlement type="city">Lyon</settlement>
<region type="region" nuts="2">Auvergne-Rhône-Alpes</region>
<region type="old region" nuts="2">Rhône-Alpes</region>
</placeName>
<orgName type="university">Université Claude Bernard Lyon 1</orgName>
<orgName type="institution" wicri:auto="newGroup">Université de Lyon</orgName>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.1021/ja801332d</idno>
<series><title level="j">Journal of the American Chemical Society</title>
<idno type="ISSN">0002-7863</idno>
<imprint><date type="datePub">2008-06-25</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"> <p>A significant fraction of proteins coded in the human proteome do not fold into stable three-dimensional structures but are either partially or completely unfolded. A key feature of this family of proteins is their proposed capacity to undergo a disorder-to-order transition upon interaction with a physiological partner. The mechanisms governing protein folding upon interaction, in particular the extent to which recognition elements are preconfigured prior to formation of molecular complexes, can prove difficult to resolve in highly flexible systems. Here, we develop a conformational model of this type of protein, using an explicit description of the unfolded state, specifically modified to allow for the presence of transient secondary structure, and combining this with extensive measurement of residual dipolar couplings throughout the chain. This combination of techniques allows us to quantitatively analyze the level and nature of helical sampling present in the interaction site of the partially folded C-terminal domain of Sendai virus nucleoprotein (N(TAIL)). Rather than fraying randomly, the molecular recognition element of N(TAIL) preferentially populates three specific overlapping helical conformers, each stabilized by an N-capping interaction. The unfolded strands adjacent to the helix are thereby projected in the direction of the partner protein, identifying a mechanism by which they could achieve nonspecific encounter interactions prior to binding. This study provides experimental evidence for the molecular basis of helix formation in partially folded peptide chains, carrying clear implications for understanding early steps of protein folding.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
<li>Norvège</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Lyon</li>
</settlement>
<orgName><li>Université Claude Bernard Lyon 1</li>
<li>Université de Lyon</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Houben, Klaartje" sort="Houben, Klaartje" uniqKey="Houben K" first="Klaartje" last="Houben">Klaartje Houben</name>
</noCountry>
<country name="Norvège"><noRegion><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>
</noRegion>
</country>
<country name="France"><noRegion><name sortKey="Lescop, Ewen" sort="Lescop, Ewen" uniqKey="Lescop E" first="Ewen" last="Lescop">Ewen Lescop</name>
</noRegion>
<name sortKey="Blackledge, Martin" sort="Blackledge, Martin" uniqKey="Blackledge M" first="Martin" last="Blackledge">Martin Blackledge</name>
<name sortKey="Blanchard, Laurence" sort="Blanchard, Laurence" uniqKey="Blanchard L" first="Laurence" last="Blanchard">Laurence Blanchard</name>
<name sortKey="Ruigrok, Rob W H" sort="Ruigrok, Rob W H" uniqKey="Ruigrok R" first="Rob W H" last="Ruigrok">Rob W H. Ruigrok</name>
</country>
</tree>
</affiliations>
</record>
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