PDBsum entry 2mjm

Signaling protein, protein binding

PDB id: 2mjm

Contents

Protein chain

101 a.a.

PDB id:

2mjm

Name:

Signaling protein, protein binding

Title:

The solution nmr structure of the nlrc5 caspase recruitment domain (card)

Structure:

Protein nlrc5. Chain: a. Fragment: nlrc5 caspase recruitment domain (unp residues 1-96). Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: nlrc5. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

P.G.M.Gutte,O.Zerbe

Key ref:

P.G.Gutte et al. (2014). Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain. Biochemistry, 53, 3106-3117. PubMed id: 24815518 DOI: 10.1021/bi500177x

Date:

12-Jan-14 Release date: 03-Sep-14

Protein chain

C3VPR6  (NLRC5_MOUSE) -  Protein NLRC5 from Mus musculus

Seq: 1915 a.a.

Struc: 101 a.a.

DOI no: 10.1021/bi500177x

Biochemistry 53:3106-3117 (2014)

PubMed id: 24815518

Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.

P.G.Gutte, S.Jurt, M.G.Grütter, O.Zerbe.

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 α-helix bundle with a general death fold, though it displays specific structural features that are strikingly different from the CARD. Notably, α-helix 3 is replaced by an ordered loop, and α-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.