Structure of the PRYSPRY-domain: implications for autoinflammatory diseases.

We determined the first structure of PRYSPRY, a domain found in over 500 different proteins, involved in innate immune signaling, cytokine signaling suppression, development, cell growth and retroviral restriction. The fold encompasses a 7-stranded and a 6-stranded antiparallel beta-sheet, arranged in a beta-sandwich. In the crystal, PRYSPRY forms a dimer ...
where the C-terminus of an acceptor molecule binds to the concave surface of a donor molecule, which represents a putative interaction site. Mutations in the PRYSPRY domains of Pyrin, which are responsible for familial Mediterranean fever, map on the putative PRYSPRY interaction site.
Mesh Terms:
Amino Acid Motifs, Autoimmune Diseases, Cytoskeletal Proteins, Dimerization, Humans, Immunity, Innate, Inflammation, Mutation, Protein Binding, Protein Structure, Tertiary, Retroviridae, Signal Transduction, Structural Homology, Protein
FEBS Lett.
Date: Jan. 09, 2006
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