 |
PDBsum entry 4cio
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
RNA binding protein/RNA
|
PDB id
|
|
|
|
4cio
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Backbone-Independent nucleic acid binding by splicing factor sup-12 reveals key aspects of molecular recognition.
|
|
|
Authors
|
|
S.Amrane,
K.Rebora,
I.Zniber,
D.Dupuy,
C.D.Mackereth.
|
|
|
Ref.
|
|
Nat Commun, 2014,
5,
4595.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Cellular differentiation is frequently accompanied by alternative splicing,
enabled by the expression of tissue-specific factors which bind to pre-mRNAs and
regulate exon choice. During Caenorhabditis elegans development, muscle-specific
expression of the splicing factor SUP-12, together with a member of the Fox-1
family of splicing proteins, generates a functionally distinct isoform of the
fibroblast growth factor receptor EGL-15. Using a combination of NMR
spectroscopy and isothermal titration calorimetry, we determined the mode of
nucleic acid binding by the RNA recognition motif domain of SUP-12. The
calculated structures provide the first atomic details of RNA and DNA binding by
the family of proteins that include SUP-12, RBM24, RBM38/RNPC1, SEB-4 and
XSeb4R. This information was further used to design strategic mutations to probe
the interaction with ASD-1 and to quantitatively perturb splicing in vivo.
|
|
|
|
|
|
|
