Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A.
The crystal structure of the RNA binding domain of the U1 small nuclear ribonucleoprotein A, which forms part of the ribonucleoprotein complex involved in the excision of introns, has been solved. It contains a four-stranded beta sheet and two alpha helices. The highly conserved segments designated RNP1 and RNP2 lie side by side on the middle two beta strands. U1 RNA binding studies of mutant proteins suggest that the RNA binds to the four-stranded beta sheet and to the flexible loops on one end.
Nagai
K
K
MRC Laboratory of Molecular Biology, Cambridge, UK.
Oubridge
C
C
Jessen
T H
TH
Li
J
J
Evans
P R
PR
D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000648:ultrastructure*; D003001:Cloning, Molecular; D003196:Computer Graphics; D003461:Crystallography; D004252:DNA Mutational Analysis; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D012326:RNA Splicing; D012342:RNA, Small Nuclear / Q000378:metabolism*; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins / Q000648:ultrastructure*; D017411:Ribonucleoproteins, Small Nuclear; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D012342:RNA, Small Nuclear; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D017411:Ribonucleoproteins, Small Nuclear