Crystal structure of a Pumilio homology domain

Mol Cell. 2001 Apr;7(4):855-65. doi: 10.1016/s1097-2765(01)00229-5.

Abstract

Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • Crystallography
  • Drosophila
  • Drosophila Proteins*
  • Humans
  • Insect Proteins / chemistry*
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Molecular Sequence Data
  • Multigene Family
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • Drosophila Proteins
  • Insect Proteins
  • RNA, Messenger
  • RNA-Binding Proteins
  • Transcription Factors
  • pum protein, Drosophila

Associated data

  • PDB/1IB2
  • PDB/1IB3