利用酶促反应构建拓扑蛋白质连接。 - Suppr

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Making topological protein links using enzymatic reactions.

作者信息

Castells-Graells Roger, Yeates Todd O

机构信息

Department of Chemistry and Biochemistry, University of California, USA.

UCLA-DOE Institute for Genomics and Proteomics, USA.

出版信息

Natl Sci Rev. 2024 Apr 3;11(3):nwae071. doi: 10.1093/nsr/nwae071. eCollection 2024 Mar.

DOI:10.1093/nsr/nwae071

PMID:38572076

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10990160/

Abstract

摘要

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84d/10990160/941e83f236f5/nwae071fig1.jpg

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Cellular Synthesis and X-ray Crystal Structure of a Designed Protein Heterocatenane.

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KnotProt 2.0: a database of proteins with knots and other entangled structures.

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相似文献

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本文引用的文献

A single-domain protein catenane of dihydrofolate reductase.

Natl Sci Rev. 2023 Nov 29;10(11):nwad304. doi: 10.1093/nsr/nwad304. eCollection 2023 Nov.

De novo design of knotted tandem repeat proteins.

Nat Commun. 2023 Oct 24;14(1):6746. doi: 10.1038/s41467-023-42388-y.

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Science. 2022 Oct 7;378(6615):49-56. doi: 10.1126/science.add2187. Epub 2022 Sep 15.

Cellular Synthesis and X-ray Crystal Structure of a Designed Protein Heterocatenane.

Angew Chem Int Ed Engl. 2020 Sep 7;59(37):16122-16127. doi: 10.1002/anie.202005490. Epub 2020 Jul 9.

KnotProt 2.0: a database of proteins with knots and other entangled structures.

Nucleic Acids Res. 2019 Jan 8;47(D1):D367-D375. doi: 10.1093/nar/gky1140.

Structure and folding of a designed knotted protein.

Proc Natl Acad Sci U S A. 2010 Nov 30;107(48):20732-7. doi: 10.1073/pnas.1007602107. Epub 2010 Nov 10.

Discovery of a thermophilic protein complex stabilized by topologically interlinked chains.

J Mol Biol. 2007 May 18;368(5):1332-44. doi: 10.1016/j.jmb.2007.02.078. Epub 2007 Mar 6.

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Biochemistry. 2003 Dec 30;42(51):15148-57. doi: 10.1021/bi035338v.

Angew Chem Int Ed Engl. 2001 Oct 1;40(19):3625-3627. doi: 10.1002/1521-3773(20011001)40:19<3625::aid-anie3625>3.0.co;2-q.

A deeply knotted protein structure and how it might fold.

Nature. 2000 Aug 24;406(6798):916-9. doi: 10.1038/35022623.