title: A novel RING finger in the C-terminal domain of the coatomer protein α-COP.
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.
authors.affiliation: CSIR-Institute of Microbial Technology (IMTECH), Sector 39-A, Chandigarh, 160036, India. gurmeetkaur@imtech.res.in.
authors.forename: Gurmeet
authors.initials: G
authors.lastname: Kaur
authors.affiliation: CSIR-Institute of Microbial Technology (IMTECH), Sector 39-A, Chandigarh, 160036, India. krishna@imtech.res.in.
authors.forename: Srikrishna
authors.initials: S
authors.lastname: Subramanian
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle / Q000235:genetics*; D020756:Coatomer Protein / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D016335:Zinc Fingers
chemical_list: D020756:Coatomer Protein; D029701:Saccharomyces cerevisiae Proteins