1t2r | pdb_00001t2r
From Proteopedia
Structural basis for 3' end recognition of nucleic acids by the Drosophila Argonaute 2 PAZ domain
| ||||||||||||
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3'-terminal nucleotides are buried in a hydrophobic cleft. We propose that the PAZ domain contributes to the specific recognition of siRNAs by providing a binding pocket for their characteristic two-nucleotide 3' overhangs. Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.,Lingel A, Simon B, Izaurralde E, Sattler M Nat Struct Mol Biol. 2004 Jun;11(6):576-7. Epub 2004 May 23. PMID:15156196[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
Contents | ||||||||||||||||||
This page was last modified 21:29, 29 September 2014.