期刊
MOLECULAR CELL
卷 6, 期 2, 页码 373-384出版社
CELL PRESS
DOI: 10.1016/S1097-2765(00)00037-X
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资金
- NIDDK NIH HHS [DK49207] Funding Source: Medline
- NIGMS NIH HHS [R01 GM056846, GM56846] Funding Source: Medline
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)P-4, the head group of the major PI 3-K product PtdIns(3,4,5)P-3. One of these PH domains (from Grp1) is PtdIns(3,4,5)P-3 specific, while the other (from DAPP1/PHISH) binds strongly to both Ptdlns(3,4,5)P-3 and its 5'-dephosphorylation product, Ptdlns(3,4)P-2. 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.
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