2LEB

Solution structure of human SRSF2 (SC35) RRM in complex with 5'-UCCAGU-3'

Summary for 2LEB

• Entry DOI: 10.2210/pdb2leb/pdb
• Related: 2LEA 2LEC
• NMR Information: BMRB: 17706
• Descriptor: Serine/arginine-rich splicing factor 2, RNA (5'-R(*UP*CP*CP*AP*GP*U)-3') (2 entities in total)
• Functional Keywords: sr protein, splicing factor, rna protein complex, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q01130
• Total number of polymer chains: 2
• Total formula weight: 17110.22

Authors

Daubner, G.M.,Clery, A.,Jayne, S.,Stevenin, J.,Allain, F.H.-T. (deposition date: 2011-06-15, release date: 2011-11-23, Last modification date: 2024-05-08)

Primary citation

Daubner, G.M.,Clery, A.,Jayne, S.,Stevenin, J.,Allain, F.H.
A syn-anti conformational difference allows SRSF2 to recognize guanines and cytosines equally well.
Embo J., 31:162-174, 2012

PubMed Abstract: SRSF2 (SC35) is a key player in the regulation of alternative splicing events and binds degenerated RNA sequences with similar affinity in nanomolar range. We have determined the solution structure of the SRSF2 RRM bound to the 5'-UCCAGU-3' and 5'-UGGAGU-3' RNA, both identified as SRSF2 binding sites in the HIV-1 tat exon 2. RNA recognition is achieved through a novel sandwich-like structure with both termini forming a positively charged cavity to accommodate the four central nucleotides. To bind both RNA sequences equally well, SRSF2 forms a nearly identical network of intermolecular interactions by simply flipping the bases of the two consecutive C or G nucleotides into either anti or syn conformation. We validate this unusual mode of RNA recognition functionally by in-vitro and in-vivo splicing assays and propose a 5'-SSNG-3' (S=C/G) high-affinity binding consensus sequence for SRSF2. In conclusion, in addition to describe for the first time the RNA recognition mode of SRSF2, we provide the precise consensus sequence to identify new putative binding sites for this splicing factor.

PubMed: 22002536
DOI: 10.1038/emboj.2011.367

Experimental method

SOLUTION NMR