3fmo
From Proteopedia
Contents |
Crystal structure of the nucleoporin Nup214 in complex with the DEAD-box helicase Ddx19
Template:ABSTRACT PUBMED 19208808
Disease
[NU214_HUMAN] Note=A chromosomal aberration involving NUP214 is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It results in the formation of a DEK-CAN fusion gene. Note=A chromosomal aberration involving NUP214 is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with SET.
Function
[NU214_HUMAN] May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex. [DD19B_HUMAN] ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.
About this Structure
3fmo is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Napetschnig J, Kassube SA, Debler EW, Wong RW, Blobel G, Hoelz A. Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19. Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3089-94. Epub 2009 Feb 10. PMID:19208808
Categories: Homo sapiens | Blobel, G. | Debler, E W. | Hoelz, A. | Napetschnig, J. | Atp-binding | Beta-propeller | Dead box | Glycoprotein | Helicase | Hydrolase | Membrane | Mrna export | Mrna transport | Nuclear pore complex | Nuclear porin | Nucleocytoplasmic transport | Nucleotide-binding | Nucleus | Oncoprotein-hydrolase complex | Phosphoprotein | Protein interaction | Protein transport | Protein transport-hydrolase complex | Proto-oncogene | Rna-binding | Translocation | Transport