Abstract:
:The cocrystal structure of human poly(A)-binding protein (PABP) has been determined at 2.6 A resolution. PABP recognizes the 3' mRNA poly(A) tail and plays critical roles in eukaryotic translation initiation and mRNA stabilization/degradation. The minimal PABP used in this study consists of the N-terminal two RRM-type RNA-binding domains connected by a short linker (RRM1/2). These two RRMs form a continuous RNA-binding trough, lined by an antiparallel beta sheet backed by four alpha helices. The polyadenylate RNA adopts an extended conformation running the length of the molecular trough. Adenine recognition is primarily mediated by contacts with conserved residues found in the RNP motifs of the two RRMs. The convex dorsum of RRM1/2 displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with translation initiation factors and regulatory proteins.
journal_name
Celljournal_title
Cellauthors
Deo RC,Bonanno JB,Sonenberg N,Burley SKdoi
10.1016/s0092-8674(00)81517-2subject
Has Abstractpub_date
1999-09-17 00:00:00pages
835-45issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81517-2journal_volume
98pub_type
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