Related ArticlesThe N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
J Mol Biol. 1999 Jul 9;290(2):495-504
Authors: Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The N-terminal region of HsRad51 is highly conserved among eukaryotic Rad51 proteins but is absent from RecA, suggesting a Rad51-specific function for this region. Here, we have determined the structure of the N-terminal part of HsRad51 by NMR spectroscopy. The N-terminal region forms a compact domain consisting of five short helices, which shares structural similarity with a domain of endonuclease III, a DNA repair enzyme of E. coli. NMR experiments did not support the involvement of the N-terminal domain in HsRad51-HsBrca2 interaction or the self-association of HsRad51 as proposed by previous studies. However, NMR tiration experiments demonstrated a physical interaction of the domain with DNA, and allowed mapping of the DNA binding surface. Mutation analysis showed that the DNA binding surface is essential for double-stranded and single-stranded DNA binding of HsRad51. Our results suggest the presence of a DNA binding site on the outside surface of the HsRad51 filament and provide a possible explanation for the regulation of DNA binding by phosphorylation within the N-terminal domain.
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Related Articles NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Eur J Biochem. 1999 Dec;266(2):359-69
Authors: Wecker K, Roques BP
The human immunodeficiency virus type 1 (HIV-1) genome encodes a highly conserved 16 kDa regulatory gene product, Vpr (viral protein of regulation, 96 amino acid residues), which is incorporated into virions, in quantities equivalent to those of the viral Gag proteins. In the infected cells, Vpr is...
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[NMR paper] NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotei
NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Related Articles NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Protein Eng. 1998 Oct;11(10):847-53
Authors: McAlister MS, Davis B, Pfuhl M, Driscoll PC
CD5 is a type-I transmembrane glycoprotein found on thymocytes, T-cells and a subset of B-cells. The extracellular region consists of three domains belonging to the...
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[NMR paper] Structure determination of the N-terminal thioredoxin-like domain of protein disulfid
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Biochemistry. 1996 Jun 18;35(24):7684-91
Authors: Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE
As a first step in...
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[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev
NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Biochemistry. 1994 May 17;33(19):6004-14
Authors: Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL
The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...
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[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev
NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Biochemistry. 1994 May 17;33(19):6004-14
Authors: Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL
The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...
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[NMR paper] NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A pro
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
EMBO J. 1994 Aug 15;13(16):3873-81
Authors: Howe PW, Nagai K, Neuhaus D, Varani G
The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70-90...
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[NMR paper] NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: m
NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
J Mol Biol. 1999 Feb 5;285(5):2105-17
Authors: Schüler W, Wecker K, de Rocquigny H, Baudat Y, Sire J, Roques BP
The HIV-1 regulatory protein Vpr (96 amino...
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA bindi
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