Related ArticlesUnusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Biochemistry. 2014 May 20;53(19):3106-17
Authors: Gutte PG, Jurt S, Grütter MG, Zerbe O
Abstract
The cytosolic nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs) are key sensors for bacterial and viral invaders and endogenous stress signals. NLRs contain a varying N-terminal effector domain that regulates the downstream signaling events upon its activation and determines the subclass to which a NLR member belongs. NLRC5 contains an unclassified N-terminal effector domain that has been reported to interact downstream with the tandem caspase recruitment domain (CARD) of retinoic acid-inducible gene I (RIG-I). Here we report the solution structure of the N-terminal effector domain of NLRC5 and in vitro interaction experiments with the tandem CARD of RIG-I. The N-terminal effector domain of NLRC5 adopts a six ?-helix bundle with a general death fold, though it displays specific structural features that are strikingly different from the CARD. Notably, ?-helix 3 is replaced by an ordered loop, and ?-helix 1 is devoid of the characteristic interruption. Detailed structural alignments between the N-terminal effector domains of NLRC5 with a representative of each death-fold subfamily showed that NLRC5 fits best to the CARD subfamily and can be called an atypical CARD. Due to the specific structural features, the atypical CARD also displays a different electrostatic surface. Because the shape and charge of the surface is crucial for the establishment of a homotypic CARD-CARD interaction, these specific structural features seem to have a significant effect on the interaction between the atypical CARD of NLRC5 and the tandem RIG-I CARD.
[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Related Articles Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Publication date: Available online 15 May 2014
Source:Structure</br>
Author(s): Alessandro*A. Rizzo , Margaret*M. Suhanovsky , Matthew*L. Baker , LaTasha*C.R. Fraser , Lisa*M. Jones , Don*L. Rempel , Michael*L. Gross , Wah Chiu , Andrei*T. Alexandrescu , Carolyn*M. Teschke</br>
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique...
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05-15-2014 07:23 PM
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500177x/aop/images/medium/bi-2014-00177x_0007.gif
Biochemistry
DOI: 10.1021/bi500177x
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/0XcYOsOxzfs
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05-09-2014 07:01 PM
[NMR paper] Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
PLoS One. 2013;8(9):e74040
Authors: Huan X, Shi J, Lim L, Mitra S, Zhu W, Qin H, Pasquale EB, Song J
Abstract
The 16 EphA and EphB receptors represent the largest family of receptor tyrosine kinases, and their interactions...
[NMR paper] NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro
NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
Related Articles NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
J Mol Biol. 2000 Jan 28;295(4):729-36
Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E
The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR....
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[NMR paper] Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Related Articles Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Biochemistry. 1995 May 16;34(19):6488-503
Authors: Borer PN, Lin Y, Wang S, Roggenbuck MW, Gott JM, Uhlenbeck OC, Pelczer I
The three-dimensional conformation of a 24-nucleotide variant of the RNA binding sequence for the coat protein of bacteriophage R17 has been analyzed using NMR, molecular dynamics, and energy minimization. The imino proton spectrum is consistent with base pairing...
Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Linear Mode
