1D9A

SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN (RBD2) OF HU ANTIGEN C (HUC)

Summary for 1D9A

• Entry DOI: 10.2210/pdb1d9a/pdb
• Related: 1D8Z
• Descriptor: HU ANTIGEN C (1 entity in total)
• Functional Keywords: rna-binding domain, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 9351.66

Authors

Inoue, M.,Muto, Y.,Sakamoto, H.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1999-10-26, release date: 2000-04-07, Last modification date: 2024-05-22)

Primary citation

Inoue, M.,Muto, Y.,Sakamoto, H.,Yokoyama, S.
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.
Nucleic Acids Res., 28:1743-1750, 2000

PubMed 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.

PubMed: 10734193
DOI: 10.1093/nar/28.8.1743

Experimental method

SOLUTION NMR