1M8Y

CRYSTAL STRUCTURE OF THE PUMILIO-HOMOLOGY DOMAIN FROM HUMAN PUMILIO1 IN COMPLEX WITH NRE2-10 RNA

Summary for 1M8Y

• Entry DOI: 10.2210/pdb1m8y/pdb
• Related: 1IB2 1IB3 1M8W 1M8X
• Descriptor: 5'-R(P*AP*UP*UP*GP*UP*AP*CP*AP*UP*A)-3', Pumilio 1 (3 entities in total)
• Functional Keywords: pumilio-homology domain, puf domain, nanos response element, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (Probable): Q14671
• Total number of polymer chains: 4
• Total formula weight: 87022.88

Authors

Wang, X.,McLachlan, J.,Zamore, P.D.,Hall, T.M.T. (deposition date: 2002-07-26, release date: 2002-09-25, Last modification date: 2024-02-14)

Primary citation

Wang, X.,McLachlan, J.,Zamore, P.D.,Hall, T.M.T.
MODULAR RECOGNITION OF RNA BY A HUMAN PUMILIO-HOMOLOGY DOMAIN
CELL(CAMBRIDGE,MASS.), 110:501-512, 2002

PubMed 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.

PubMed: 12202039
DOI: 10.1016/S0092-8674(02)00873-5

Experimental method

X-RAY DIFFRACTION (2.6 Å)