Literature summary for 2.7.7.19 extracted from

Nakel, K.; Bonneau, F.; Basquin, C.; Habermann, B.; Eckmann, C.R.; Conti, E.
Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity (2016), RNA, 22, 1139-1145.

Crystallization (Commentary)

Crystallization (Comment)	Organism
core complex of isoform GLD-2 and RRM RNA binding domain protein RNP-8, to 2.5 A resolution. RNP-8 embraces the poly(A)-polymerase, docking onto several conserved hydrophobic hotspots present on the GLD-2 surface. RNP-8 stabilizes GLD-2 and indirectly stimulates polyadenylation. RNP-8 differs in amino-acid sequence and structure from GLD-2 binding partner GLD-3 but binds the same surfaces of GLD-2 by forming alternative interactions	Caenorhabditis elegans

Crystallization (Comment)

Organism

core complex of isoform GLD-2 and RRM RNA binding domain protein RNP-8, to 2.5 A resolution. RNP-8 embraces the poly(A)-polymerase, docking onto several conserved hydrophobic hotspots present on the GLD-2 surface. RNP-8 stabilizes GLD-2 and indirectly stimulates polyadenylation. RNP-8 differs in amino-acid sequence and structure from GLD-2 binding partner GLD-3 but binds the same surfaces of GLD-2 by forming alternative interactions

Caenorhabditis elegans

Organism

Organism	UniProt	Comment	Textmining
Caenorhabditis elegans	O17087	-	-

Synonyms

Synonyms	Comment	Organism
GLD-2	-	Caenorhabditis elegans

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Release 2023.1 (January 2023)