3v69
From Proteopedia
Filia-N crystal structure
Structural highlights
Function[KHDC3_MOUSE] Required for maintenance of euploidy during cleavage-stage embryogenesis. Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process. Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function. Capable of binding RNA.[1] [2] Publication Abstract from PubMedFILIA is a member of the recently identified oocyte/embryo expressed gene family in eutherian mammals, which is characterized by containing an N-terminal atypical KH domain. Here we report the structure of the N-terminal fragment of FILIA (FILIA-N), which represents the first reported three-dimensional structure of a KH domain in the oocyte/embryo expressed gene family of proteins. The structure of FILIA-N revealed a unique N-terminal extension beyond the canonical KH region, which plays important roles in interaction with RNA. By co-incubation with the lysates of mice ovaries, FILIA and FILIA-N could sequester specific RNA components, supporting the critical roles of FILIA in regulation of RNA transcripts during mouse oogenesis and early embryogenesis. The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA.,Wang J, Xu M, Zhu K, Li L, Liu X PLoS One. 2012;7(1):e30209. Epub 2012 Jan 19. PMID:22276159[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Lk3 transgenic mice | Li, L | Liu, X | Wang, J | Xu, M | Zhu, K | Embryogenesis | Filia | Kh domain | Protein binding | Rna binding | Rna-binding
