1m8y | pdb_00001m8y

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

spinqualitylabelsall models 1m8y, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m8y is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ib3, 1ib2, 1m8w, 1m8x Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PUM1_HUMAN] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Modular recognition of RNA by a human pumilio-homology domain.,Wang X, McLachlan J, Zamore PD, Hall TM Cell. 2002 Aug 23;110(4):501-12. PMID:12202039 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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