2hh2
From Proteopedia
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'''Solution structure of the fourth KH domain of KSRP''' | '''Solution structure of the fourth KH domain of KSRP''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Garcia-Mayoral, M F.]] | [[Category: Garcia-Mayoral, M F.]] | ||
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Revision as of 03:17, 4 May 2008
Solution structure of the fourth KH domain of KSRP
Overview
The AU-rich element (ARE) RNA-binding protein KSRP (K-homology splicing regulator protein) contains four KH domains and promotes the degradation of specific mRNAs that encode proteins with functions in cellular proliferation and inflammatory response. The fourth KH domain (KH4) is essential for mRNA recognition and decay but requires the third KH domain (KH3) for its function. We show that KH3 and KH4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of KSRP. This provides KSRP with the structural flexibility needed to recognize a set of different targets in the context of their 3'UTR structural settings. Surprisingly, we find that KH4 binds to its target AREs with lower affinity than KH3 and that KSRP's mRNA binding, and mRNA degradation activities are closely associated with a conserved structural element of KH4.
About this Structure
2HH2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation., Garcia-Mayoral MF, Hollingworth D, Masino L, Diaz-Moreno I, Kelly G, Gherzi R, Chou CF, Chen CY, Ramos A, Structure. 2007 Apr;15(4):485-98. PMID:17437720 Page seeded by OCA on Sun May 4 06:17:04 2008
