Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Angiogenic Proteins / chemistry*
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Angiogenic Proteins / metabolism*
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Hydrocarbons, Aromatic / chemistry
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Hydrocarbons, Aromatic / metabolism
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Intracellular Signaling Peptides and Proteins / chemistry*
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Intracellular Signaling Peptides and Proteins / metabolism*
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Pattern Recognition, Automated / methods
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Protein Structure, Tertiary
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RNA / chemistry*
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RNA / metabolism*
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Sequence Alignment / methods
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Sequence Analysis, Protein / methods*
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
Substances
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AGGF1 protein, human
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Angiogenic Proteins
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Hydrocarbons, Aromatic
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Intracellular Signaling Peptides and Proteins
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RBM14 protein, human
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RNA