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Structure of the PRYSPRY‐domain: Implications for autoinflammatory diseases
Author(s) -
Grütter Christian,
Briand Christophe,
Capitani Guido,
Mittl Peer R.E.,
Papin Stephanie,
Tschopp Jürg,
Grütter Markus G.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.076
Subject(s) - pyrin domain , antiparallel (mathematics) , innate immune system , inflammasome , dimer , protein structure , biology , familial mediterranean fever , chemistry , microbiology and biotechnology , genetics , immune system , receptor , biochemistry , medicine , physics , organic chemistry , quantum mechanics , magnetic field , disease , pathology
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 β‐sheet, arranged in a β‐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.