It is increasingly recognized that very small proteins (?-proteins) are ubiquitously found in all species of the three domains of life, and that they fulfill important functions. The halophilic archaeon Haloferax volcanii contains 282 ?-proteins of less than 70 amino acids. Notably, 43 of these contain two C(P)XCG motifs, suggesting their potential to complex a zinc ion. To explore the significance of these proteins, 16 genes encoding C(P)XCG proteins had been deleted, and the majority of...
[NMR paper] Zinc finger structure determination by NMR: Why zinc fingers can be a handful
Zinc finger structure determination by NMR: Why zinc fingers can be a handful
Zinc fingers can be loosely defined as protein domains containing one or more tetrahedrally-co-ordinated zinc ions whose role is to stabilise the structure rather than to be involved in enzymatic chemistry; such zinc ions are often referred to as "structural zincs". Although structural zincs can occur in proteins of any size, they assume particular significance for very small protein domains, where they are often essential for maintaining a folded state. Such small structures, that sometimes...
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[NMR paper] Biological functions, genetic and biochemical characterization, and NMR structure determination of the small zinc finger protein HVO_2753 from Haloferax volcanii.
Biological functions, genetic and biochemical characterization, and NMR structure determination of the small zinc finger protein HVO_2753 from Haloferax volcanii.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Biological functions, genetic and biochemical characterization, and NMR structure determination of the small zinc finger protein HVO_2753 from Haloferax volcanii.
FEBS J. 2020 Sep 09;:
Authors: Zahn S, Kubatova N, Pyper DJ, Cassidy L, Saxena K, Tholey A, Schwalbe H,...
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[ASAP] Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01055/20200220/images/medium/bi9b01055_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01055
http://feeds.feedburner.com/~r/acs/bichaw/~4/un5QBZFhB-o
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[ASAP] Unraveling the RNA Binding Properties of the Iron–Sulfur Zinc Finger Protein CPSF30
Unraveling the RNA Binding Properties of the Iron–Sulfur Zinc Finger Protein CPSF30
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01065/20200219/images/medium/bi9b01065_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01065
http://feeds.feedburner.com/~r/acs/bichaw/~4/gciyur7Eemg
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[NMR paper] Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation.
Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation.
Related Articles Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation.
Proteins. 2017 Feb 03;:
Authors: Zhu J, Wang H, Ramelot TA, Kennedy MA, Hu R, Yue X, Liu M, Yang Y
Abstract
Human INSM1 containing five C-terminal C2H2-type zinc fingers (ZFs), is a key regulator of neuroendocrine development. Previous research reported that full-length...
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[NMR paper] Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
PLoS One. 2013;8(1):e52908
Authors: Guillière F, Danioux C, Jaubert C, Desnoues N, Delepierre M, Prangishvili D, Sezonov G, Guijarro JI
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[NMR paper] NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine
NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Related Articles NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Biochemistry. 1999 Oct 5;38(40):12984-94
Authors: Schüler W, Dong C, Wecker K, Roques BP
The structure of the 56 amino acid nucleocapsid protein NCp10 of...
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[NMR paper] Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger o
Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR...
Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure
Linear Mode
