Structure of the PRYSPRY-domain:: Implications for autoinflammatory diseases

被引：73

作者：

Grütter, C

Briand, C

Capitani, G

Mittl, PRE

Papin, S

Tschopp, E

Grütter, MG

机构：

[1] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland

[2] Univ Lausanne, Dept Biochem, CH-1066 Epalinges, Switzerland

来源：

FEBS LETTERS | 2006年 / 580卷 / 01期

关键词：

PRYSPRY; crystal structure; FMF diseases; multiple wavelength anomalous dispersion;

D O I：

10.1016/j.febslet.2005.11.076

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2005 Federation of European Biochemical Societies. Publised by Elsevier B.V. All rights reserved.

引用

页码：99 / 106

页数：8

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