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The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domains.

Abstract:

The yeast splicing factor Prp40 (pre-mRNA processing protein 40) consists of a pair of WW domains followed by several FF domains. The region comprising the FF domains has been shown to associate with the 5' end of U1 small nuclear RNA and to interact directly with two proteins, the Clf1 (Crooked neck-like factor 1) and the phosphorylated repeats of the C-terminal domain of RNA polymerase II (CTD-RNAPII). In this work we reported the solution structure of the first FF domain of Prp40 and the i...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.M508047200

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Journal:
The Journal of biological chemistry
Volume:
281
Issue:
1
Pages:
356-364
Publication date:
2006-01-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:c7e82342-570f-4da8-8f36-c65a4bc9bc2d
Source identifiers:
386476
Local pid:
pubs:386476

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