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4B92

Crystal structure of truncated human CRMP-5 soaked with Zn

4B92 の概要
エントリーDOI10.2210/pdb4b92/pdb
関連するPDBエントリー4B90 4B91
分子名称DIHYDROPYRIMIDINASE-RELATED PROTEIN 5, ZINC ION (3 entities in total)
機能のキーワードsignaling protein, neurogenesis, phosphoprotein, crmp, tim barrel, axonal outgrowth, developmental protein
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Cytoplasm (Probable): Q9BPU6
タンパク質・核酸の鎖数2
化学式量合計106168.63
構造登録者
Ponnusamy, R.,Lohkamp, B. (登録日: 2012-08-31, 公開日: 2013-02-13, 最終更新日: 2023-12-20)
主引用文献Ponnusamy, R.,Lohkamp, B.
Insights Into the Oligomerization of Crmps: Crystal Structure of Human Collapsin Response Mediator Protein 5.
J.Neurochem., 125:855-, 2013
Cited by
PubMed Abstract: Collapsin response mediator protein-5 (CRMP-5) is the latest identified member of the CRMP cytosolic phosphoprotein family, which is crucial for neuronal development and repair. CRMPs exist as homo- and/or hetero-tetramers in vivo and participate in signaling transduction, cytoskeleton rearrangements, and endocytosis. CRMP-5 antagonizes many of the other CRMPs' functions either by directly interacting with them or by competing for their binding partners. We determined the crystal structures of a full length and a truncated version of human CRMP-5, both of which form a homo-tetramer similar to those observed in CRMP-1 and CRMP-2. However, solution studies indicate that CRMP-5 and CRMP-1 form weaker homo-tetramers compared with CRMP-2, and that divalent cations, Ca(2+) and Mg(2+), destabilize oligomers of CRMP-5 and CRMP-1, but promote CRMP-2 oligomerization. On the basis of comparative analysis of the CRMP-5 crystal structure, we identified residues that are crucial for determining the preference for hetero-oligomer or homo-oligomer formation. We also show that in spite of being the CRMP family member most closely related to dihydropyrimidinase, CRMP-5 does not have any detectable amidohydrolase activity. The presented findings provide new detailed insights into the structure, oligomerization, and regulation of CRMPs.
PubMed: 23373749
DOI: 10.1111/JNC.12188
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 4b92
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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