2MMY

Solution structure of the RNA recognition motif of human TAF15

2MMY の概要

• エントリーDOI: 10.2210/pdb2mmy/pdb
• NMR情報: BMRB: 19320
• 分子名称: TATA-binding protein-associated factor 2N (1 entity in total)
• 機能のキーワード: taf15, rrm, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q92804
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10619.90

構造登録者

Kashyap, M.,Ganguly, A.K.,Bhavesh, N.S. (登録日: 2014-03-22, 公開日: 2015-03-25, 最終更新日: 2024-05-15)

主引用文献

Kashyap, M.,Ganguly, A.K.,Bhavesh, N.S.
Structural delineation of stem-loop RNA binding by human TAF15 protein
Sci Rep, 5:17298-17298, 2015

PubMed Abstract: Human TATA binding protein associated factor 2 N (TAF15) and Fused in sarcoma (FUS) are nucleic acid binding proteins belonging to the conserved FET family of proteins. They are involved in diverse processes such as pre-mRNA splicing, mRNA transport, and DNA binding. The absence of information regarding the structural mechanism employed by the FET family in recognizing and discriminating their cognate and non-cognate RNA targets has hampered the attainment of consensus on modes of protein-RNA binding for this family. Our study provides a molecular basis of this RNA recognition using a combination of solution-state NMR spectroscopy, calorimetry, docking and molecular dynamics simulation. Analysis of TAF15-RRM solution structure and its binding with stem-loop RNA has yielded conclusive evidence of a non-canonical mode of RNA recognition. Rather than classical stacking interactions that occur across nitrogen bases and aromatic amino acids on ribonucleoprotein sites, moderate-affinity hydrogen bonding network between the nitrogen bases in the stem-loop RNA and a concave face on the RRM surface primarily mediate TAF15-RRM RNA interaction. We have compared the binding affinities across a set of single-stranded RNA oligonucleotides to conclusively establish that RNA binding is dependent upon structural elements in the RNA rather than sequence.

PubMed: 26612539
DOI: 10.1038/srep17298

実験手法

SOLUTION NMR