2QKD
Crystal structure of tandem ZPR1 domains
2QKD の概要
| エントリーDOI | 10.2210/pdb2qkd/pdb |
| 分子名称 | Zinc finger protein ZPR1, ZINC ION, FORMIC ACID, ... (4 entities in total) |
| 機能のキーワード | helical hairpins, beta helix, anti-parrallel beta sheet, double straded anti-parallel beta helix, metal binding protein, signaling protein, cell cycle |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Cytoplasm: Q62384 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 45631.80 |
| 構造登録者 | |
| 主引用文献 | Mishra, A.K.,Gangwani, L.,Davis, R.J.,Lambright, D.G. Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes. Proc.Natl.Acad.Sci.Usa, 104:13930-13935, 2007 Cited by PubMed Abstract: Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes. PubMed: 17704259DOI: 10.1073/pnas.0704915104 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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