2NZ7

Crystal Structure Analysis of Caspase-recruitment Domain (CARD) of Nod1

Summary for 2NZ7

• Entry DOI: 10.2210/pdb2nz7/pdb
• Descriptor: Caspase recruitment domain-containing protein 4 (2 entities in total)
• Functional Keywords: helix swapped; disulfide bond, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y239
• Total number of polymer chains: 2
• Total formula weight: 22730.01

Authors

Thiagarajan, S.,Robbins, S.L.,Dubas, R.L.,Park, Y.C. (deposition date: 2006-11-22, release date: 2007-12-04, Last modification date: 2024-10-16)

Primary citation

Srimathi, T.,Robbins, S.L.,Dubas, R.L.,Hasegawa, M.,Inohara, N.,Park, Y.C.
Monomer/dimer transition of the caspase-recruitment domain of human Nod1
Biochemistry, 47:1319-1325, 2008

PubMed Abstract: Nod1 is an essential cytoplasmic sensor for bacterial peptidoglycans in the innate immune system. The caspase-recruitment domain of Nod1 (Nod1_CARD) is indispensable for recruiting a downstream kinase, receptor-interacting protein 2 (RIP2), that activates nuclear factor-kappaB (NF-kappaB). The crystal structure of human Nod1_CARD at 1.9 A resolution reveals a novel homodimeric conformation. Our structural and biochemical analysis shows that the homodimerization of Nod1_CARD is achieved by swapping the H6 helices at the carboxy termini and stabilized by forming an interchain disulfide bond between the Cys39 residues of the two monomers in solution and in the crystal. In addition, we present experimental evidence for a pH-sensitive conformational change of Nod1_CARD. Our results suggest that the pH-sensitive monomer/dimer transition is a unique molecular property of Nod1_CARD.

PubMed: 18186648
DOI: 10.1021/bi7016602

Experimental method

X-RAY DIFFRACTION (1.9 Å)