Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
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DOI：
10.1016/s1097-2765(03)00115-1
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发表时间：
2003-04-01
期刊：
影响因子：
16
通讯作者：
Sattler, M
中科院分区：
文献类型：
--
作者：
Selenko, P;Gregorovic, G;Sattler, M
The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF 65 complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.
