3V69

Filia-N crystal structure

Summary for 3V69

• Entry DOI: 10.2210/pdb3v69/pdb
• Descriptor: Protein Filia (2 entities in total)
• Functional Keywords: filia, rna-binding, embryogenesis, kh domain, rna binding, protein binding
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm, cell cortex: Q9CWU5
• Total number of polymer chains: 2
• Total formula weight: 33350.74

Authors

Wang, J.,Xu, M.,Zhu, K.,Li, L.,Liu, X. (deposition date: 2011-12-19, release date: 2012-02-15, Last modification date: 2024-03-20)

Primary citation

Wang, J.,Xu, M.,Zhu, K.,Li, L.,Liu, X.
The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA.
Plos One, 7:e30209-e30209, 2012

PubMed Abstract: FILIA 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.

PubMed: 22276159
DOI: 10.1371/journal.pone.0030209

Experimental method

X-RAY DIFFRACTION (2.2 Å)