17ra
From Proteopedia
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BRANCHPOINT HELIX FROM YEAST AND BINDING SITE FOR PHAGE GA/MS2 COAT PROTEINS, NMR, 12 STRUCTURES
Overview
The RNA molecules that make up the spliceosome branch-point helix and the, binding site for phage GA coat protein share a secondary structure motif, in which two consecutive adenine residues occupy the strand opposite a, single uridine, creating the potential to form one of two different A.U, base pairs while leaving the other adenine unpaired or bulged. During the, splicing of introns out of pre-mRNA, the 2'-OH of the bulged adenine, participates in the transesterification reaction at the 5'-exon and forms, the branch-point residue of the lariat intermediate. Either adenine may, act as the branch-point residue in mammals, but the 3'-proximal adenine, does so preferentially. When bound to phage GA coat protein, the bulged, adenine loops out of the helix and occupies a binding pocket on ... [(full description)]
About this Structure
17RA is a [Protein complex] structure of sequences from [[1]]. Structure known Active Site: AAU. Full crystallographic information is available from [OCA].
Reference
NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein., Smith JS, Nikonowicz EP, Biochemistry. 1998 Sep 29;37(39):13486-98. PMID:9753434
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