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3HWJ

Crystal structure of the second PHR domain of Mouse Myc-binding protein 2 (MYCBP-2)

3HWJ の概要
エントリーDOI10.2210/pdb3hwj/pdb
関連するPDBエントリー3GBW
分子名称E3 ubiquitin-protein ligase MYCBP2, DIMETHYL SULFOXIDE (3 entities in total)
機能のキーワードmyc-binding protein 2, mycbp2, phr proteins, phr domain, probable e3 ubiquitin-protein ligase mycbp2, protein associated with myc, pam, phr1, structural genomics, psi-2, protein structure initiative, new york structural genomix research consortium, nysgxrc, alternative splicing, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation pathway, zinc, zinc-finger, new york sgx research center for structural genomics
由来する生物種Mus musculus (mouse)
タンパク質・核酸の鎖数2
化学式量合計38181.45
構造登録者
主引用文献Sampathkumar, P.,Ozyurt, S.A.,Miller, S.A.,Bain, K.T.,Rutter, M.E.,Gheyi, T.,Abrams, B.,Wang, Y.,Atwell, S.,Luz, J.G.,Thompson, D.A.,Wasserman, S.R.,Emtage, J.S.,Park, E.C.,Rongo, C.,Jin, Y.,Klemke, R.L.,Sauder, J.M.,Burley, S.K.
Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1.
J.Mol.Biol., 397:883-892, 2010
Cited by
PubMed Abstract: PHR [PAM (protein associated with Myc)-HIW (Highwire)-RPM-1 (regulator of presynaptic morphology 1)] proteins are conserved, large multi-domain E3 ubiquitin ligases with modular architecture. PHR proteins presynaptically control synaptic growth and axon guidance and postsynaptically regulate endocytosis of glutamate receptors. Dysfunction of neuronal ubiquitin-mediated proteasomal degradation is implicated in various neurodegenerative diseases. PHR proteins are characterized by the presence of two PHR domains near the N-terminus, which are essential for proper localization and function. Structures of both the first and second PHR domains of Mus musculus (mouse) Phr1 (MYC binding protein 2, Mycbp2) have been determined, revealing a novel beta sandwich fold composed of 11 antiparallel beta-strands. Conserved loops decorate the apical side of the first PHR domain (MmPHR1), yielding a distinct conserved surface feature. The surface of the second PHR domain (MmPHR2), in contrast, lacks significant conservation. Importantly, the structure of MmPHR1 provides insights into a loss-of-function mutation, Gly1092-->Glu, observed in the Caenorhabditis elegans ortholog RPM-1.
PubMed: 20156452
DOI: 10.1016/j.jmb.2010.02.017
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.25 Å)
構造検証レポート
Validation report summary of 3hwj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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