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3FEH

Crystal structure of full length centaurin alpha-1

3FEH の概要
エントリーDOI10.2210/pdb3feh/pdb
分子名称Centaurin-alpha-1, ZINC ION, UNKNOWN ATOM OR ION, ... (4 entities in total)
機能のキーワードstructural genomics consortium, gap, gtpase activation, sgc, metal-binding, nucleus, phosphoprotein, zinc-finger, metal binding protein, hydrolase activator
由来する生物種Homo sapiens (man)
細胞内の位置Nucleus: O75689
タンパク質・核酸の鎖数1
化学式量合計45065.19
構造登録者
主引用文献Tong, Y.,Tempel, W.,Wang, H.,Yamada, K.,Shen, L.,Senisterra, G.A.,Mackenzie, F.,Chishti, A.H.,Park, H.W.
Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1.
Proc.Natl.Acad.Sci.USA, 107:20346-20351, 2010
Cited by
PubMed Abstract: Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin α1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.
PubMed: 21057110
DOI: 10.1073/pnas.1009008107
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 3feh
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2025-06-11に公開中

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