Solution NMR structure of the TRIM21 B-box2 and identification of residues involved in its interaction with the RING domain.
PLoS One. 2017;12(7):e0181551
Authors: Wallenhammar A, Anandapadamanaban M, Lemak A, Mirabello C, Lundström P, Wallner B, Sunnerhagen M
Abstract
Tripartite motif-containing (TRIM) proteins are defined by the sequential arrangement of RING, B-box and coiled-coil domains (RBCC), where the B-box domain is a unique feature of the TRIM protein family. TRIM21 is an E3 ubiquitin-protein ligase implicated in innate immune signaling by acting as an autoantigen and by modifying interferon regulatory factors. Here we report the three-dimensional solution structure of the TRIM21 B-box2 domain by nuclear magnetic resonance (NMR) spectroscopy. The structure of the B-box2 domain, comprising TRIM21 residues 86-130, consists of a short ?-helical segment with an N-terminal short ?-strand and two anti-parallel ?-strands jointly found the core, and adopts a RING-like fold. This ???? core largely defines the overall fold of the TRIM21 B-box2 and the coordination of one Zn2+ ion stabilizes the tertiary structure of the protein. Using NMR titration experiments, we have identified an exposed interaction surface, a novel interaction patch where the B-box2 is likely to bind the N-terminal RING domain. Our structure together with comparisons with other TRIM B-box domains jointly reveal how its different surfaces are employed for various modular interactions, and provides extended understanding of how this domain relates to flanking domains in TRIM proteins.
[NMR paper] Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
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Biomol NMR Assign. 2015 May 13;
Authors: Nogueira ML, Sforça ML, Chin YK, Mobli M, Handler A, Gorbatyuk VY, Robson SA, King GF, Gueiros-Filho FJ, Zeri AC
Abstract
Bacterial division begins with the...
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Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
...
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09-10-2011 06:51 PM
[NMR paper] NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
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J Am Chem Soc. 2005 Sep 14;127(36):12620-6
Authors: Torizawa T, Ono AM, Terauchi T, Kainosho M
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/15N-labeled...
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12-01-2010 06:56 PM
[NMR paper] High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice
High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides.
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J Biol Chem. 2003 Apr 25;278(17):15341-8
Authors: Katoh S, Hong C, Tsunoda Y, Murata K, Takai R, Minami E, Yamazaki T, Katoh E
EL5, a RING-H2 finger protein, is rapidly induced by...
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11-24-2010 09:01 PM
[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
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J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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[NMR paper] Identification of residues involved in the interaction of Staphylococcus aureus fibro
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
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Biochemistry. 2000 Mar 21;39(11):2887-93
Authors: Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR
Many...
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11-18-2010 09:15 PM
NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
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[NMR paper] The solution NMR structure of glucosylated N-glycans involved in the early stages of
The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding.
EMBO J. 1997 Jul 16;16(14):4302-10
Authors: Petrescu AJ, Butters TD, Reinkensmeier G, Petrescu S, Platt FM, Dwek RA, Wormald MR
Glucosylated oligomannose N-linked...