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Structural basis for the interaction between unfarnesylated progerin and the Ig-like domain of lamin A/C in premature aging disorders
DC Field | Value | Language |
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dc.contributor.author | Ahn, Jinsook | - |
dc.contributor.author | Lee, Jinwook | - |
dc.contributor.author | Jeong, Soyeon | - |
dc.contributor.author | Jo, Inseong | - |
dc.contributor.author | Kang, So-mi | - |
dc.contributor.author | Park, Bum-Joon | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.date.accessioned | 2023-04-18T06:29:26Z | - |
dc.date.available | 2023-04-18T06:29:26Z | - |
dc.date.created | 2022-12-26 | - |
dc.date.created | 2022-12-26 | - |
dc.date.created | 2022-12-26 | - |
dc.date.created | 2022-12-26 | - |
dc.date.created | 2022-12-26 | - |
dc.date.issued | 2022-12 | - |
dc.identifier.citation | Biochemical and Biophysical Research Communications, Vol.637, pp.210-217 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://hdl.handle.net/10371/190110 | - |
dc.description.abstract | © 2022 Elsevier Inc.Hutchinson–Gilford progeria syndrome (HGPS) is a premature aging disorder caused by C-terminally truncated lamin A, termed as the pre-progerin product. Progerin is a C-terminally farnesylated protein derived from pre-progerin, which causes nuclear deformation at the inner-nuclear membrane. As an alternative or additional mechanism, a farnesylation-independent abnormal interaction between the C-terminus of progerin and Ig-like domain has been proposed. However, the molecular mechanism underlying the role of unfarnesylated C-terminus of pre-progerin in HGPS remains largely unknown. In this study, we determined the crystal structures of C-terminal peptide of progerin and Ig-like domain of lamin A/C. Results showed that the C-terminal cysteine residue of progerin forms a disulfide bond with the only cysteine residue of the Ig-like domain. This finding suggested that unfarnesylated progerin can form a disulfide bond with the Ig-like domain in the lamin meshwork. The Alphafold2-assisted docking structure showed that disulfide bond formation was promoted by a weak interaction between the groove of Ig-like domain and the unfarnesylated C-terminal tail region of progerin. Our results provide molecular insights into the normal aging process as well as premature aging of humans. | - |
dc.language | 영어 | - |
dc.publisher | Elsevier B.V. | - |
dc.title | Structural basis for the interaction between unfarnesylated progerin and the Ig-like domain of lamin A/C in premature aging disorders | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbrc.2022.10.070 | - |
dc.citation.journaltitle | Biochemical and Biophysical Research Communications | - |
dc.identifier.wosid | 000905124300007 | - |
dc.identifier.scopusid | 2-s2.0-85142147583 | - |
dc.citation.endpage | 217 | - |
dc.citation.startpage | 210 | - |
dc.citation.volume | 637 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Ha, Nam-Chul | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
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