{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T11:15:11Z","timestamp":1760267711179,"version":"build-2065373602"},"reference-count":48,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2019,9,11]],"date-time":"2019-09-11T00:00:00Z","timestamp":1568160000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"IDEX Paris-Saclay","award":["ANR-11-IDEX-0003-02"],"award-info":[{"award-number":["ANR-11-IDEX-0003-02"]}]},{"name":"GENCI-CINES","award":["A0040710415"],"award-info":[{"award-number":["A0040710415"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Cellular regulation or signaling processes are mediated by many proteins which often have one or several intrinsically disordered regions (IDRs). These IDRs generally serve as binders to different proteins with high specificity. In many cases, IDRs undergo a disorder-to-order transition upon binding, following a mechanism between two possible pathways, the induced fit or the conformational selection. Since these mechanisms contribute differently to the kinetics of IDR associations, it is important to investigate them in order to gain insight into the physical factors that determine the biomolecular recognition process. The verprolin homology domain (V) of the Neural Wiskott\u2013Aldrich Syndrome Protein (N-WASP), involved in the regulation of actin polymerization, is a typical example of IDR. It is composed of two WH2 motifs, each being able to bind one actin molecule. In this study, we investigated the early steps of the recognition process of actin by the WH2 motifs of N-WASP domain V. Using docking calculations and molecular dynamics simulations, our study shows that actin is first recognized by the N-WASP domain V regions which have the highest propensity to form transient    \u03b1   -helices. The WH2 motif consensus sequences \u201cLKKV\u201d subsequently bind to actin through large conformational changes of the disordered domain V.<\/jats:p>","DOI":"10.3390\/ijms20184493","type":"journal-article","created":{"date-parts":[[2019,9,11]],"date-time":"2019-09-11T11:26:34Z","timestamp":1568201194000},"page":"4493","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Investigation into Early Steps of Actin Recognition by the Intrinsically Disordered N-WASP Domain V"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7801-087X","authenticated-orcid":false,"given":"Maud","family":"Chan-Yao-Chong","sequence":"first","affiliation":[{"name":"BioCIS, University Paris-Sud, CNRS UMR 8076, University Paris-Saclay, 92290 Ch\u00e2tenay-Malabry, France"},{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, University Paris-Saclay, 91190 Gif-sur-Yvette, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9414-5857","authenticated-orcid":false,"given":"Dominique","family":"Durand","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, University Paris-Saclay, 91190 Gif-sur-Yvette, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0847-2948","authenticated-orcid":false,"given":"T\u00e2p","family":"Ha-Duong","sequence":"additional","affiliation":[{"name":"BioCIS, University Paris-Sud, CNRS UMR 8076, University Paris-Saclay, 92290 Ch\u00e2tenay-Malabry, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,9,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/jmbi.1999.3110","article-title":"Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm","volume":"293","author":"Wright","year":"1999","journal-title":"J. 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