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PDBsum entry 6id1
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1981 a.a.
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888 a.a.
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303 a.a.
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568 a.a.
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475 a.a.
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290 a.a.
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272 a.a.
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159 a.a.
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317 a.a.
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347 a.a.
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97 a.a.
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74 a.a.
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79 a.a.
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74 a.a.
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132 a.a.
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67 a.a.
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152 a.a.
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576 a.a.
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1322 a.a.
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79 a.a.
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85 a.a.
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67 a.a.
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162 a.a.
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94 a.a.
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663 a.a.
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References listed in PDB file
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Key reference
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Title
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Structures of the human spliceosomes before and after release of the ligated exon.
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Authors
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X.Zhang,
X.Zhan,
C.Yan,
W.Zhang,
D.Liu,
J.Lei,
Y.Shi.
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Ref.
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Cell Res, 2019,
29,
274-285.
[DOI no: ]
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PubMed id
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Abstract
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Pre-mRNA splicing is executed by the spliceosome, which has eight major
functional states each with distinct composition. Five of these eight human
spliceosomal complexes, all preceding exon ligation, have been structurally
characterized. In this study, we report the cryo-electron microscopy structures
of the human post-catalytic spliceosome (P complex) and intron lariat
spliceosome (ILS) at average resolutions of 3.0 and 2.9 Å, respectively. In
the P complex, the ligated exon remains anchored to loop I of U5 small nuclear
RNA, and the 3'-splice site is recognized by the junction between the 5'-splice
site and the branch point sequence. The ATPase/helicase Prp22, along with the
ligated exon and eight other proteins, are dissociated in the P-to-ILS
transition. Intriguingly, the ILS complex exists in two distinct conformations,
one with the ATPase/helicase Prp43 and one without. Comparison of these three
late-stage human spliceosomes reveals mechanistic insights into exon release and
spliceosome disassembly.
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