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.
Grütter
Christian
C
Department of Biochemistry, University of Zürich, CH-8057 Zürich, Switzerland.
Briand
Christophe
C
Capitani
Guido
G
Mittl
Peer R E
PR
Papin
Stephanie
S
Tschopp
Jürg
J
Grütter
Markus G
MG
D020816:Amino Acid Motifs / Q000235:genetics / Q000276:immunology; D001327:Autoimmune Diseases / Q000235:genetics / Q000276:immunology; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D019281:Dimerization; D006801:Humans; D007113:Immunity, Innate / Q000235:genetics; D007249:Inflammation / Q000235:genetics / Q000276:immunology; D009154:Mutation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D000071198:Pyrin; D012190:Retroviridae / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D015398:Signal Transduction / Q000276:immunology; D040681:Structural Homology, Protein
D003598:Cytoskeletal Proteins; C000604192:MEFV protein, human; D000071198:Pyrin