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Structure of the PRYSPRY-domain: implications for autoinflammatory diseases
Christian Grütter1, Christophe Briand, Guido Capitani
1Department of Biochemistry, University of Zürich, CH-8057 Zürich, Switzerland.
Abstract:
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.
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