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1M8X

CRYSTAL STRUCTURE OF THE PUMILIO-HOMOLOGY DOMAIN FROM HUMAN PUMILIO1 IN COMPLEX WITH NRE1-14 RNA

Summary for 1M8X
Entry DOI10.2210/pdb1m8x/pdb
Related1IB2 1IB3 1M8W 1M8Y
Descriptor5'-R(P*UP*UP*GP*UP*AP*UP*AP*U)-3', 5'-R(P*UP*GP*UP*AP*UP*AP*U)-3', Pumilio 1, ... (4 entities in total)
Functional Keywordspumilio-homology domain, puf domain, nanos response element, rna binding protein-rna complex, rna binding protein/rna
Biological sourceHomo sapiens (human)
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Cellular locationCytoplasm (Probable): Q14671
Total number of polymer chains4
Total formula weight85401.86
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 citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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