OCRE: a novel domain made of imperfect, aromatic-rich octamer repeats
Isabelle Callebaut1, Jean-Paul Mornon
1Département de Biologie Structurale, LMCP, CNRS UMR7590, Universités Paris 6 & Paris 7, Case 115, 4 place Jussieu, 75252 Paris Cedex 05, France. Isabelle. Callebaut@lmcp.jussieu.fr
Summary:
In this study, we describe a novel domain, OCRE, which is shared by the recently identified angiogenic factor VG5Q and a specific family of RNA-binding motif proteins. The OCRE domain is characterized by a 5-fold, imperfectly repeated octameric sequence, which includes a triplet of often-conserved aromatic amino acids predicted to form a beta-strand and in which the slightly modified fifth repeat might act as a repeat terminator. Although the function of this domain remains to be elucidated, the domain architecture of OCRE containing proteins and experimental data suggest a role in RNA metabolism and/or in signalling pathways activated by the tumor necrosis factor superfamily of cytokines.
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