Structure of the PRYSPRY-domain: Implications for autoinflammatory diseases
| Autor: | Guido Capitani, Christophe Briand, Stephanie Papin, Christian Grütter, Peer R. E. Mittl, Jürg Tschopp, Markus G. Grütter |
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| Jazyk: | angličtina |
| Předmět: |
Amino Acid Motifs
Biophysics Familial Mediterranean fever Biology Antiparallel (biochemistry) Biochemistry Pyrin domain Autoimmune Diseases Multiple wavelength anomalous dispersion FMF diseases Structural Biology Concave surface Genetics medicine Humans Molecular Biology Inflammation Innate immune system Crystal structure A domain Interaction site Cell Biology Pyrin medicine.disease PRYSPRY Immunity Innate Protein Structure Tertiary Cytoskeletal Proteins Retroviridae Structural Homology Protein Mutation Dimerization Protein Binding Signal Transduction |
| Zdroj: | FEBS Letters. (1):99-106 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2005.11.076 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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