PROSITE documentation PDOC51544 [for PROSITE entry PS51544]

Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile




Description

Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate 4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in turns, initiates a vast array of signaling events. PI3Ks can be grouped into three classes based on their domain organization. Class I PI3Ks are heterodimers consisting of a p110 catalytic subunit and a regulatory subunit of either the p85 type (associated with the class IA p110 isoforms p110α, p110β or p110delta) or the p101 type (associated with the class IB p110 isoform p110γ). Common to all catalytic subunits are the N-terminal adaptor-binding domain (ABD) that binds to p85, the Ras-binding domain (RBD) (see <PDOC51546>), the putative membrane-binding domain (C2), the helical domain of unknown function, and the kinase catalytic domain (see <PDOC00710>) [1,2,3].

PI3K ABD is a small globular domain of about 100 residues in length with an α/β-sandwich topology (see <PDB:2RD0>) [1,2,3].

The profile we developed covers the entire PI3K ABD domain.

Last update:

July 2011 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PI3K_ABD, PS51544; Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile  (MATRIX)


References

1AuthorsMiled N., Yan Y., Hon W.-C., Perisic O., Zvelebil M., Inbar Y., Schneidman-Duhovny D., Wolfson H.J., Backer J.M., Williams R.L.
TitleMechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.
SourceScience 317:239-242(2007).
PubMed ID17626883
DOI10.1126/science.1135394

2AuthorsHuang C.-H., Mandelker D., Schmidt-Kittler O., Samuels Y., Velculescu V.E., Kinzler K.W., Vogelstein B., Gabelli S.B., Amzel L.M.
TitleThe structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.
SourceScience 318:1744-1748(2007).
PubMed ID18079394
DOI10.1126/science.1150799

3AuthorsBerndt A., Miller S., Williams O., Le D.D., Houseman B.T., Pacold J.I., Gorrec F., Hon W.-C., Liu Y., Rommel C., Gaillard P., Rueckle T., Schwarz M.K., Shokat K.M., Shaw J.P., Williams R.L.
TitleThe p110delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors.
SourceNat. Chem. Biol. 6:244-244(2010).
PubMed ID20154668
DOI10.1038/nchembio0310-244b



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