Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052214 | FEBS Letters | 2006 | 8 Pages |
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 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.
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Authors
Christian Grütter, Christophe Briand, Guido Capitani, Peer R.E. Mittl, Stephanie Papin, Jürg Tschopp, Markus G. Grütter,