3fe2
From Proteopedia
Human DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADP
Structural highlights
Function[DDX5_HUMAN] Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] Publication Abstract from PubMedDEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members. Comparative structural analysis of human DEAD-box RNA helicases.,Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364[11] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
Categories: Homo sapiens | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Bountra, C | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Persson, C | Structural genomic | Sagemark, J | Schuler, H | Siponen, M I | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | Wisniewska, M | Adp | Atp-binding | Dead | Helicase | Hydrolase | Methylation | Mrna processing | Mrna splicing | Nucleotide-binding | Nucleus | Phosphoprotein | Rna helicase | Rna-binding | Sgc | Spliceosome
