OCRE: a novel domain made of imperfect, aromatic-rich octamer repeats.
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.
Département 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
Isabelle
I
Callebaut
Jean-Paul
JP
Mornon
D042501:Angiogenic Proteins / Q000737:chemistry* / Q000378:metabolism*; D006841:Hydrocarbons, Aromatic / Q000737:chemistry / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry* / Q000378:metabolism*; D010363:Pattern Recognition, Automated / Q000379:methods; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment / Q000379:methods; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
C482200:AGGF1 protein, human; D042501:Angiogenic Proteins; D006841:Hydrocarbons, Aromatic; D047908:Intracellular Signaling Peptides and Proteins; C436317:RBM14 protein, human; D012313:RNA