PDBsum entry 2n00

DNA binding protein

PDB id: 2n00

Contents

Protein chain

95 a.a.

PDB id:

2n00

Name:

DNA binding protein

Title:

Nmr solution structure of aim2 pyd from mus musculus

Structure:

Interferon-inducible protein aim2. Chain: a. Fragment: unp residues 1-95. Synonym: interferon-inducible protein 210, ifi-210, interferon- inducible protein p210. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: aim2, gm1313, ifi210. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

X.Hou,X.Niu

Key ref:

X.Hou and X.Niu (2015). The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct α2-α3 helix conformation from its human homologues. Biochem Biophys Res Commun, 461, 396-400. PubMed id: 25888795 DOI: 10.1016/j.bbrc.2015.04.046

Date:

01-Mar-15 Release date: 27-May-15

Protein chain

Q91VJ1  (AIM2_MOUSE) -  Interferon-inducible protein AIM2 from Mus musculus

Seq: 354 a.a.

Struc: 95 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.bbrc.2015.04.046

Biochem Biophys Res Commun 461:396-400 (2015)

PubMed id: 25888795

The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct α2-α3 helix conformation from its human homologues.

X.Hou, X.Niu.

ABSTRACT

The inflammasome is a key component of the innate immune system providing the initial defense against invading organisms. Failure of inflammasome formation is the main reason for many innate and acquired immune diseases. Cytosolic protein absent in melanoma 2 (AIM2) has been reported to play an essential role in double-stranded DNA (dsDNA) sensing and inflammasome formation in response to viruses or bacteria infection. The N-terminal pyrin domain (PYD) of AIM2 interacts with the ASC PYD domain, and then recruits downstream proteins to assemble the AIM2 inflammasome. The molecular mechanisms of PYD mediated signaling remain elusive as limited structural information on PYD family. Herein, we characterized the solution structure of mouse AIM2 PYD domain by NMR spectroscopy, and compared it with the crystal structures of its two human homologues. The comparison shows mAIM2 PYD adopts a unique α2-α3 helix conformation distinct from its human homologues, but similar to the pyrin domain of human NLRP10/PYNOD, which belongs to another family. In addition, the aggregation of mAIM2 PYD domain, with the increased salt concentration, reveals that both the charge surface and hydrophobic interaction play important roles in the self-association of mAIM2 PYD.