Backbone and sidechain methyl Ile (delta1), Leu and Val resonance assignments of the catalytic domain of the yeast mRNA decapping enzyme, Dcp2.
Eukaryotic mRNA decapping by Dcp2 is the penultimate step in several mRNA decay pathways. To understand regulation of Dcp2 by ligand interactions, we have assigned the backbone and sidechain methyl Ile (delta1), Leu and Val chemical shifts of the catalytic domain of the S. Cerevisiae enzyme.
Deshmukh
Mandar V
MV
Department Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, S-512E, Box 2280, San Francisco, CA 94158, USA.
Oku
Yuko
Y
Gross
John D
JD
D020134:Catalytic Domain; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics; D007532:Isoleucine / Q000031:analogs & derivatives / Q000737:chemistry; D007930:Leucine / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics; D014633:Valine / Q000737:chemistry
D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C030052:mRNA decapping enzymes; D007532:Isoleucine; C400572:DCP2 protein, S cerevisiae; D004722:Endoribonucleases; D007930:Leucine; D014633:Valine