PDBsum entry 1d8z

RNA binding protein

PDB id: 1d8z

Contents

Protein chain

89 a.a. *

* Residue conservation analysis

PDB id:

1d8z

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

Date:

26-Oct-99 Release date: 07-Apr-00

Protein chain

Q60900  (ELAV3_MOUSE) -  ELAV-like protein 3 from Mus musculus

Seq: 367 a.a.

Struc: 89 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

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.

ABSTRACT

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.