Summary information and primary citation
- PDB-id
-
1m8y;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- RNA binding protein-RNA
- Method
- X-ray (2.6 Å)
- Summary
- Crystal structure of the pumilio-homology domain from
human pumilio1 in complex with nre2-10 RNA
- Reference
-
Wang X, McLachlan J, Zamore PD, Hall TMT (2002):
"MODULAR
RECOGNITION OF RNA BY A HUMAN PUMILIO-HOMOLOGY
DOMAIN." CELL(CAMBRIDGE,MASS.),
110, 501-512. doi: 10.1016/S0092-8674(02)00873-5.
- Abstract
- Puf proteins are developmental regulators that control
mRNA stability and translation by binding sequences in the
3' untranslated regions of their target mRNAs. We have
determined the structure of the RNA binding domain of the
human Puf protein, Pumilio1, bound to a high-affinity RNA
ligand. The RNA binds the concave surface of the molecule,
where each of the protein's eight repeats makes contacts
with a different RNA base via three amino acid side chains
at conserved positions. We have mutated these three side
chains in one repeat, thereby altering the sequence
specificity of Pumilio1. Thus, the high affinity and
specificity of the PUM-HD for RNA is achieved using
multiple copies of a simple repeated motif.
