PDBsum entry 1d8z

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protein links
RNA binding protein PDB id
Protein chain
89 a.a. *
* Residue conservation analysis
PDB id:
Name: RNA binding protein
Title: Solution structure of the first RNA-binding domain (rbd1) of hu antigen c (huc)
Structure: Hu antigen c. Chain: a. Fragment: first RNA-binding domain (rbd1). Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 1 models
Authors: M.Inoue,Y.Muto,H.Sakamoto,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: M.Inoue et al. (2000). NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C. Nucleic Acids Res, 28, 1743-1750. PubMed id: 10734193 DOI: 10.1093/nar/28.8.1743
26-Oct-99     Release date:   07-Apr-00    
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Protein chain
Pfam   ArchSchema ?
Q60900  (ELAV3_MOUSE) -  ELAV-like protein 3
367 a.a.
89 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleotide binding     3 terms  


DOI no: 10.1093/nar/28.8.1743 Nucleic Acids Res 28:1743-1750 (2000)
PubMed id: 10734193  
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.
M.Inoue, Y.Muto, H.Sakamoto, S.Yokoyama.
Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3'-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1-RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1-RBD2 were mapped on and around the two beta-sheets and on the C-terminal region of RBD1. The HuC RBD1-RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1-RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18581050 M.N.Hinman, and H.Lou (2008).
Diverse molecular functions of Hu proteins.
  Cell Mol Life Sci, 65, 3168-3181.  
17517897 E.J.Fialcowitz-White, B.Y.Brewer, J.D.Ballin, C.D.Willis, E.A.Toth, and G.M.Wilson (2007).
Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences.
  J Biol Chem, 282, 20948-20959.  
12773396 J.M.Pérez Cañadillas, and G.Varani (2003).
Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein.
  EMBO J, 22, 2821-2830.
PDB code: 1p1t
12388766 P.Björk, G.Baurén, S.Jin, Y.G.Tong, T.R.Bürglin, U.Hellman, and L.Wieslander (2002).
A novel conserved RNA-binding domain protein, RBD-1, is essential for ribosome biogenesis.
  Mol Biol Cell, 13, 3683-3695.  
11179892 J.M.Pérez-Cañadillas, and G.Varani (2001).
Recent advances in RNA-protein recognition.
  Curr Opin Struct Biol, 11, 53-58.  
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