1FAO

STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH IN COMPLEX WITH INOSITOL 1,3,4,5-TETRAKISPHOSPHATE

1FAO の概要

• エントリーDOI: 10.2210/pdb1fao/pdb
• 関連するPDBエントリー: 1FB8
• 分子名称: DUAL ADAPTOR OF PHOSPHOTYROSINE AND 3-PHOSPHOINOSITIDES, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE (3 entities in total)
• 機能のキーワード: pleckstrin, 3-phosphoinositides, inositol tetrakisphosphate signal transduction protein, adaptor protein, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15305.10

構造登録者

Ferguson, K.M.,Kavran, J.M.,Sankaran, V.G.,Fournier, E.,Isakoff, S.J.,Skolnik, E.Y.,Lemmon, M.A. (登録日: 2000-07-13, 公開日: 2000-07-20, 最終更新日: 2024-10-30)

主引用文献

Ferguson, K.M.,Kavran, J.M.,Sankaran, V.G.,Fournier, E.,Isakoff, S.J.,Skolnik, E.Y.,Lemmon, M.A.
Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.
Mol.Cell, 6:373-384, 2000

PubMed Abstract: Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal-dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two different PH domains bound to Ins(1,3,4,5)P4, the head group of the major PI 3-K product PtdIns(3,4,5)P3. One of these PH domains (from Grp1) is PtdIns(3,4,5)P3 specific, while the other (from DAPP1/PHISH) binds strongly to both PtdIns(3,4,5)P3 and its 5'-dephosphorylation product, PtdIns(3,4)P2. Comparison of the two structures provides an explanation for the distinct phosphoinositide specificities of the two PH domains and allows us to predict the 3-phosphoinositide selectivity of uncharacterized PH domains.

PubMed: 10983984
DOI: 10.1016/S1097-2765(00)00037-X

実験手法

X-RAY DIFFRACTION (1.8 Å)