Structure of the PRYSPRY-domain: implications for autoinflammatory diseases

Christian Grütter; Christophe Briand; Guido Capitani; Peer R E Mittl; Stephanie Papin; Jürg Tschopp; Markus G Grütter

doi:10.1016/j.febslet.2005.11.076

Structure of the PRYSPRY-domain: implications for autoinflammatory diseases

FEBS Lett. 2006 Jan 9;580(1):99-106. doi: 10.1016/j.febslet.2005.11.076. Epub 2005 Dec 9.

Authors

Christian Grütter¹, Christophe Briand, Guido Capitani, Peer R E Mittl, Stephanie Papin, Jürg Tschopp, Markus G Grütter

Affiliation

¹ Department of Biochemistry, University of Zürich, CH-8057 Zürich, Switzerland.

PMID: 16364311
DOI: 10.1016/j.febslet.2005.11.076

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 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Motifs / genetics
Amino Acid Motifs / immunology
Autoimmune Diseases* / genetics
Autoimmune Diseases* / immunology
Cytoskeletal Proteins / chemistry*
Cytoskeletal Proteins / genetics
Cytoskeletal Proteins / immunology
Dimerization
Humans
Immunity, Innate* / genetics
Inflammation / genetics
Inflammation / immunology
Mutation*
Protein Binding
Protein Structure, Tertiary
Pyrin
Retroviridae / chemistry
Retroviridae / genetics
Retroviridae / immunology
Signal Transduction* / immunology
Structural Homology, Protein

Substances

Cytoskeletal Proteins
MEFV protein, human
Pyrin