Structure of the PRYSPRY-domain: Implications for autoinflammatory diseases

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• 作者：Christian Grü ; tter ; Christophe Briand ; Guido Capitani ; Peer R.E. Mittl ; Stephanie Papin ; Jü ; rg Tschopp and Markus G. Grü ; tter
• 关键词：PRYSPRY ; Crystal structure ; FMF diseases ; Multiple wavelength anomalous dispersion
• 刊名：FEBS Letters
• 出版年：2006
• 出版时间：9 January 2006
• 年：2006
• 卷：580
• 期：1
• 页码：99-106
• 全文大小：1690 K

文摘

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.