Publication Abstract from PubMed
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.
Structure of the PRYSPRY-domain: implications for autoinflammatory diseases.,Grutter C, Briand C, Capitani G, Mittl PR, Papin S, Tschopp J, Grutter MG FEBS Lett. 2006 Jan 9;580(1):99-106. Epub 2005 Dec 9. PMID:16364311[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
