3FM8

Crystal structure of full length centaurin alpha-1 bound with the FHA domain of KIF13B (CAPRI target)

3FM8 の概要

• エントリーDOI: 10.2210/pdb3fm8/pdb
• 分子名称: Kinesin-like protein KIF13B, Centaurin-alpha-1, UNKNOWN ATOM OR ION, ... (6 entities in total)
• 機能のキーワード: kinesin, gap, gtpase activation, structural genomics consortium, sgc, atp-binding, cytoskeleton, microtubule, motor protein, nucleotide-binding, phosphoprotein, metal-binding, nucleus, zinc-finger, metal binding protein, transport protein-hydrolase activator complex, transport protein/hydrolase activator
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton : Q9NQT8; Nucleus: O75689
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119749.97

構造登録者

Shen, L.,Tong, Y.,Tempel, W.,MacKenzie, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Weigelt, J.,Bochkarev, A.,Park, H.,Structural Genomics Consortium (SGC) (登録日: 2008-12-19, 公開日: 2009-08-25, 最終更新日: 2024-04-03)

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 alpha1.
Proc.Natl.Acad.Sci.USA, 107:20346-20351, 2010

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

実験手法

X-RAY DIFFRACTION (2.3 Å)