{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T04:03:12Z","timestamp":1760241792876,"version":"build-2065373602"},"reference-count":51,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2018,9,25]],"date-time":"2018-09-25T00:00:00Z","timestamp":1537833600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB796, project A2"],"award-info":[{"award-number":["SFB796, project A2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001652","name":"Friedrich-Alexander-Universit\u00e4t Erlangen-N\u00fcrnberg","doi-asserted-by":"publisher","award":["funding program Open Access Publishing"],"award-info":[{"award-number":["funding program Open Access Publishing"]}],"id":[{"id":"10.13039\/501100001652","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>All herpesviruses use a heterodimeric nuclear egress complex (NEC) to transport capsids out of host cell nuclei. Despite their overall similar structure, NECs may differ significantly in sequence between different viruses. Up to now, structural information is limited to isolated NEC heterodimers and to large hexagonal lattices made up of hexagonal ring-like structures (\u201cHexagons\u201d). The present study aimed to expand the existing structural knowledge with information on the dynamics of NECs from different viruses and in different oligomerization states. For this task, comparative molecular dynamics simulations were performed of the free NEC heterodimers from three different viruses (HCMV (human cytomegalovirus), HSV-1 (herpes simplex virus 1), and PRV (pseudorabies virus)). In addition, higher oligomerization states comprising two or six NEC heterodimers were characterized for HCMV and HSV-1. The study revealed that the isolated NEC heterodimers from \u03b1- (HSV-1, PRV) and \u03b2-herpesviruses (HCMV) differ significantly in their dynamics, which can be attributed to a poorly conserved interface region between the NEC subdomains. These differences become smaller for higher oligomerization states, and both HCMV and HSV-1 individual Hexagons exhibit a common region of enhanced dynamics, which might be of functional relevance for the formation of curved vesicle structures or the recognition of hexameric capsid proteins.<\/jats:p>","DOI":"10.3390\/ijms19102908","type":"journal-article","created":{"date-parts":[[2018,9,25]],"date-time":"2018-09-25T11:12:26Z","timestamp":1537873946000},"page":"2908","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Conformational Dynamics of Herpesviral NEC Proteins in Different Oligomerization States"],"prefix":"10.3390","volume":"19","author":[{"given":"Benedikt","family":"Diewald","sequence":"first","affiliation":[{"name":"Division of Bioinformatics, Institute of Biochemistry, Friedrich-Alexander-Universit\u00e4t Erlangen-N\u00fcrnberg (FAU), Fahrstra\u00dfe 17, 91054 Erlangen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eileen","family":"Socher","sequence":"additional","affiliation":[{"name":"Division of Bioinformatics, Institute of Biochemistry, Friedrich-Alexander-Universit\u00e4t Erlangen-N\u00fcrnberg (FAU), Fahrstra\u00dfe 17, 91054 Erlangen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5839-1468","authenticated-orcid":false,"given":"Christian A.","family":"S\u00f6ldner","sequence":"additional","affiliation":[{"name":"Division of Bioinformatics, Institute of Biochemistry, Friedrich-Alexander-Universit\u00e4t Erlangen-N\u00fcrnberg (FAU), Fahrstra\u00dfe 17, 91054 Erlangen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5644-045X","authenticated-orcid":false,"given":"Heinrich","family":"Sticht","sequence":"additional","affiliation":[{"name":"Division of Bioinformatics, Institute of Biochemistry, Friedrich-Alexander-Universit\u00e4t Erlangen-N\u00fcrnberg (FAU), Fahrstra\u00dfe 17, 91054 Erlangen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2018,9,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"8988","DOI":"10.1128\/JVI.72.11.8988-9001.1998","article-title":"African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum","volume":"72","year":"1998","journal-title":"J. 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