A novel RING finger in the C-terminal domain of the coatomer protein aα-COP

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Abstract

The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization.

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Kaur, G., & Subramanian, S. (2015). A novel RING finger in the C-terminal domain of the coatomer protein aα-COP. Biology Direct, 10(1). https://doi.org/10.1186/s13062-015-0099-9

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