2FBE

Crystal Structure of the PRYSPRY-domain

Summary for 2FBE

• Entry DOI: 10.2210/pdb2fbe/pdb
• Descriptor: PREDICTED: similar to ret finger protein-like 1 (2 entities in total)
• Functional Keywords: dimer, jellyroll beta-sandwich fold, unknown function
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 89726.94

Authors

Gruetter, C.,Briand, C.,Capitani, G.,Mittl, P.R.,Gruetter, M.G. (deposition date: 2005-12-09, release date: 2006-01-10, Last modification date: 2011-07-13)

Primary citation

Gruetter, C.,Briand, C.,Capitani, G.,Mittl, P.R.,Papin, S.,Tschopp, J.,Gruetter, M.G.
Structure of the PRYSPRY-domain: Implications for autoinflammatory diseases
Febs Lett., 580:99-106, 2006

PubMed 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.

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

Experimental method

X-RAY DIFFRACTION (2.52 Å)