2RLO

Split PH domain of PI3-kinase enhancer

2RLO の概要

• エントリーDOI: 10.2210/pdb2rlo/pdb
• 分子名称: Centaurin-gamma 1 (1 entity in total)
• 機能のキーワード: split ph domain, alternative splicing, ank repeat, cytoplasm, gtp-binding, gtpase activation, metal-binding, nucleotide-binding, nucleus, oncogene, phosphorylation, polymorphism, protein transport, transport, zinc, zinc-finger, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Cytoplasm. Isoform 2: Cytoplasm: Q99490
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14328.11

構造登録者

Wen, W.,Zhang, M. (登録日: 2007-07-21, 公開日: 2008-04-29, 最終更新日: 2024-05-29)

主引用文献

Yan, J.,Wen, W.,Chan, L.N.,Zhang, M.
Split pleckstrin homology domain-mediated cytoplasmic-nuclear localization of PI3-kinase enhancer GTPase
J.Mol.Biol., 378:425-435, 2008

PubMed Abstract: Cytoplasm-nucleus shuttling of phosphoinositol 3-kinase enhancer (PIKE) is known to correlate directly with its cellular functions. However, the molecular mechanism governing this shuttling is not known. In this work, we demonstrate that PIKE is a new member of split pleckstrin homology (PH) domain-containing proteins. The structure solved in this work reveals that the PIKE PH domain is split into halves by a positively charged nuclear localization sequence. The PIKE PH domain binds to the head groups of di- and triphosphoinositides with similar affinities. Lipid membrane binding of the PIKE PH domain is further enhanced by the positively charged nuclear localization sequence, which is juxtaposed to the phosphoinositide head group-binding pocket of the domain. We demonstrate that the cytoplasmic-nuclear shuttling of PIKE is dynamically regulated by the balancing actions of the lipid-binding property of both the split PH domain and the nuclear targeting function of its nuclear localization sequence.

PubMed: 18371979
DOI: 10.1016/j.jmb.2008.02.052

実験手法

SOLUTION NMR