3KRM

Imp1 kh34

3KRM の概要

• エントリーDOI: 10.2210/pdb3krm/pdb
• 分子名称: Insulin-like growth factor 2 mRNA-binding protein 1, GLYCEROL (2 entities in total)
• 機能のキーワード: rna binding protein, kh domain, cell projection, cytoplasm, nucleus, phosphoprotein, rna-binding, translation regulation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9NZI8
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54451.89

構造登録者

Chao, J.A.,Singer, R.H.,Almo, S.C.,Patskovsky, Y. (登録日: 2009-11-18, 公開日: 2010-02-09, 最終更新日: 2024-02-21)

主引用文献

Chao, J.A.,Patskovsky, Y.,Patel, V.,Levy, M.,Almo, S.C.,Singer, R.H.
ZBP1 recognition of beta-actin zipcode induces RNA looping.
Genes Dev., 24:148-158, 2010

PubMed Abstract: ZBP1 (zipcode-binding protein 1) was originally discovered as a trans-acting factor for the "zipcode" in the 3' untranslated region (UTR) of the beta-actin mRNA that is important for its localization and translational regulation. Subsequently, ZBP1 has been found to be a multifunctional regulator of RNA metabolism that controls aspects of localization, stability, and translation for many mRNAs. To reveal how ZBP1 recognizes its RNA targets, we biochemically characterized the interaction between ZBP1 and the beta-actin zipcode. The third and fourth KH (hnRNP K homology) domains of ZBP1 specifically recognize a bipartite RNA element located within the first 28 nucleotides of the zipcode. The spacing between the RNA sequences is consistent with the structure of IMP1 KH34, the human ortholog of ZBP1, that we solved by X-ray crystallography. The tandem KH domains are arranged in an intramolecular anti-parallel pseudodimer conformation with the canonical RNA-binding surfaces at opposite ends of the molecule. This orientation of the KH domains requires that the RNA backbone must undergo an approximately 180 degrees change in direction in order for both KH domains to contact the RNA simultaneously. The RNA looping induced by ZBP1 binding provides a mechanism for specific recognition and may facilitate the assembly of post-transcriptional regulatory complexes by remodeling the bound transcript.

PubMed: 20080952
DOI: 10.1101/gad.1862910

実験手法

X-RAY DIFFRACTION (2.75 Å)