TRIADs: a new class of proteins with a novel cysteine-rich signature
Triad1 was recently identified as a nuclear RING finger protein, which is up-regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine-rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C-x(4)-C-x(14-30)-C-x(1-4)-C-x(4)-C-x(2)-C-x(4)-H-x(4)-C defines this structure as the fourth family member of the zinc-binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.
|Keywords||Amino Acid Sequence, Animals, Carrier Proteins/*chemistry, Conserved Sequence, Cysteine/*chemistry, Humans, Molecular Sequence Data, Sequence Homology, Amino Acid, Zinc Fingers|
van der Reijden, B.A., Erpelinck, C.A.J., Jansen, J.H., & Löwenberg, B.. (1999). TRIADs: a new class of proteins with a novel cysteine-rich signature. Protein Science. Retrieved from http://hdl.handle.net/1765/9139