Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Grutter C, Briand C, Capitani G, Mittl PR, Papin S, Tschopp J, Grutter MG. Structure of the PRYSPRY-domain: implications for autoinflammatory diseases. FEBS Lett. 2006 Jan 9;580(1):99-106. Epub 2005 Dec 9. PMID:16364311 doi:10.1016/j.febslet.2005.11.076