Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution (Q27654469)

3

object named as

Adelaine K W Leung

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author name string

Daniel A Pomeranz Krummel

1

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Jade Li

4

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Kiyoshi Nagai

Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism

5

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language of work or name

English

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publication date

26 March 2009

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published in

Nature

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volume

458

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issue

7237

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page(s)

475-80

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cites work

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20 March 2017

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In vitro reconstitution of mammalian U1 snRNPs active in splicing: the U1-C protein enhances the formation of early (E) spliceosomal complexes

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Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin

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The U1 snRNP protein U1C recognizes the 5' splice site in the absence of base pairing

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Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle

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The 100-kda U5 snRNP protein (hPrp28p) contacts the 5' splice site through its ATPase site

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The Mr 70,000 protein of the U1 small nuclear ribonucleoprotein particle binds to the 5' stem-loop of U1 RNA and interacts with Sm domain proteins

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The 5' end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes

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Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor

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U1-specific protein C needed for efficient complex formation of U1 snRNP with a 5' splice site

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